6oqs

<table><tr><td colspan='2'>[[6oqs]] is a 22 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OQS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6OQS FirstGlance]. <br>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">atpH, HMPREF1611_00658 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), atpA, AD31_4476 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), atpf ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), atpC, CCU01_030215 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), atpG, BN16_43751 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), atpD, CDCO157_4410 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), atpE, ECJG_03465 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), atpB, A6581_09625, A8C65_04635, A8G17_13205, A9819_21465, AC789_1c41260, ACN002_3840, ACN77_20010, ACN81_06510, ACU57_03300, ACU90_00315, AKG99_01200, AM464_11965, AMK83_17435, AML07_02005, AML35_23925, APZ14_19970, AU473_02230, AUQ13_19445, AUS26_01135, AW059_18665, AW106_23235, B1K96_28785, B7C53_19560, BANRA_02401, BANRA_03128, BANRA_03214, BANRA_04536, BANRA_04611, BB545_21600, BHF46_03220, BHS81_22305, BIZ41_19310, BK292_20055, BK400_00980, BMT53_14990, BMT91_10650, BN17_36921, BTQ04_25560, BTQ06_19305, BUE81_18230, BVL39_06790, BW690_12705, BWP17_17405, BZL31_21415, C2U48_14255, C4J69_12205, C5N07_23075, C5P01_14375, C5P43_18495, C5P44_14015, C6669_08960, C7235_25075, C7B02_15545, C7B06_18115, C7B07_18555, CA593_07300, CG691_14695, CG692_21460, CG705_13230, CG706_05505, COD30_14545, COD46_05110, CR538_25535, CR539_00375, CRD98_06365, CRE06_22220, CRM83_19985, CV83915_02325, CVH05_22810, CWS33_22485, D0X26_21590, D2F89_18645, D3821_26125, D3I61_22220, D6Z21_17295, D7K63_14130, D8K42_12760, D9D20_15080, D9D23_18435, D9D65_17115, D9D69_04800, D9D77_23770, D9E35_19420, D9F57_04785, D9G42_23250, D9H12_19550, D9H53_20710, D9H66_14770, D9H68_12120, D9H70_07975, D9H84_13135, D9I18_08055, D9I52_22315, D9I93_11990, D9J11_15870, D9J44_15620, D9J48_14640, D9K10_12565, DIV22_14605, DL800_26315, DL925_10465, DLU27_05670, DM262_10125, DMI41_02740, DNQ45_04220, DOT75_06920, DP258_23940, DP277_10610, DQF57_16240, DS732_00235, DTL43_15450, DTL90_16085, DV750_19840, E2855_04743, EAI42_11905, EAI44_10320, EAI52_06435, EB510_22250, EB553_22600, EB569_11805, EB595_21530, EC1094V2_4559, EC3234A_68c00800, EC95NR1_03180, ECs4680, ED060_20795, ED098_20360, ED124_20405, ED133_14365, ED287_08070, ED600_20035, ED648_17305, ED653_18700, ED658_09750, ED944_14625, EEP03_14120, EEP23_14845, EF364_23525, EFV06_19295, EIA21_14165, EL75_4432, EL79_4683, EL80_4591, ERS085374_04660, ERS085379_02386, ERS085383_02615, ERS085386_04244, ERS085404_04407, ERS150876_04315, FORC28_6046, GJ11_23870, HW43_00205, JD73_04915, NCTC10090_03054, NCTC10418_07533, NCTC10429_00459, NCTC10444_05020, NCTC11022_03985, NCTC11126_01888, NCTC11181_02279, NCTC13125_03147, NCTC13127_06463, NCTC13462_03577, NCTC7152_05030, NCTC8179_05398, NCTC8622_01220, NCTC8960_02611, NCTC9036_04909, NCTC9037_05079, NCTC9045_05855, NCTC9054_05546, NCTC9055_01929, NCTC9058_01885, NCTC9062_03146, NCTC9073_06659, NCTC9111_05225, NCTC9117_06282, NCTC9119_05322, NCTC9701_05266, NCTC9703_04488, NCTC9706_02267, NCTC9969_05235, PU06_21025, RG28_23995, RK56_018685, RX35_03591, SAMEA3472044_00548, SAMEA3472047_02992, SAMEA3472055_04839, SAMEA3472056_03685, SAMEA3472067_04030, SAMEA3472070_05212, SAMEA3472080_03392, SAMEA3472108_02423, SAMEA3472114_05011, SAMEA3472147_03706, SAMEA3484427_03569, SAMEA3484429_03570, SAMEA3484433_04143, SAMEA3485101_04107, SAMEA3752557_01245, SAMEA3752559_04742, SAMEA3753064_05400, SAMEA3753097_00985, SAMEA3753290_05396, SAMEA3753300_04372, SAMEA3753397_02464, SK85_04068, UN86_05680, UN91_09915, WQ89_11300, WR15_16550 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=7.1.2.2 7.1.2.2] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6oqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oqs OCA], [http://pdbe.org/6oqs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oqs RCSB], [http://www.ebi.ac.uk/pdbsum/6oqs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oqs ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/D6IFY0_ECOLX D6IFY0_ECOLX]] Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).[HAMAP-Rule:MF_01398][SAAS:SAAS00535352] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.[HAMAP-Rule:MF_01398][SAAS:SAAS00002149] [[http://www.uniprot.org/uniprot/F4TL55_ECOLX F4TL55_ECOLX]] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.[HAMAP-Rule:MF_01396] Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396] [[http://www.uniprot.org/uniprot/A0A073FQ32_ECOLX A0A073FQ32_ECOLX]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.[HAMAP-Rule:MF_01346] [[http://www.uniprot.org/uniprot/C3SL77_ECOLX C3SL77_ECOLX]] Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.[HAMAP-Rule:MF_01393][RuleBase:RU000483] [[http://www.uniprot.org/uniprot/V0ZA15_ECOLX V0ZA15_ECOLX]] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.[HAMAP-Rule:MF_01416] This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.[HAMAP-Rule:MF_01416] [[http://www.uniprot.org/uniprot/A0A4V1DSB5_ECOLX A0A4V1DSB5_ECOLX]] Produces ATP from ADP in the presence of a proton gradient across the membrane.[HAMAP-Rule:MF_00530][SAAS:SAAS00872986] [[http://www.uniprot.org/uniprot/J7RYJ3_ECOLX J7RYJ3_ECOLX]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.[HAMAP-Rule:MF_00815][SAAS:SAAS00725627]