ATP6_HAES1
ID ATP6_HAES1 Reviewed; 265 AA.
AC Q0I5W7;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=ATP synthase subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE AltName: Full=ATP synthase F0 sector subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE AltName: Full=F-ATPase subunit 6 {ECO:0000255|HAMAP-Rule:MF_01393};
GN Name=atpB {ECO:0000255|HAMAP-Rule:MF_01393}; OrderedLocusNames=HS_1702;
OS Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=205914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129Pt;
RX PubMed=17172329; DOI=10.1128/jb.01422-06;
RA Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA Xie G., Inzana T.J.;
RT "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT influenzae Rd.";
RL J. Bacteriol. 189:1890-1898(2007).
CC -!- FUNCTION: Key component of the proton channel; it plays a direct role
CC in the translocation of protons across the membrane.
CC {ECO:0000255|HAMAP-Rule:MF_01393}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. CF(1) is
CC attached to CF(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta and b chains.
CC {ECO:0000255|HAMAP-Rule:MF_01393}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01393}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01393}.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01393}.
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DR EMBL; CP000436; ABI25970.1; -; Genomic_DNA.
DR RefSeq; WP_011609846.1; NC_008309.1.
DR AlphaFoldDB; Q0I5W7; -.
DR SMR; Q0I5W7; -.
DR STRING; 205914.HS_1702; -.
DR EnsemblBacteria; ABI25970; ABI25970; HS_1702.
DR KEGG; hso:HS_1702; -.
DR eggNOG; COG0356; Bacteria.
DR HOGENOM; CLU_041018_1_0_6; -.
DR OMA; FTHAVRL; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.220; -; 1.
DR HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR InterPro; IPR045082; ATP_syn_F0_a_bact/chloroplast.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR42823; PTHR42823; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR PROSITE; PS00449; ATPASE_A; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Cell inner membrane; Cell membrane; CF(0);
KW Hydrogen ion transport; Ion transport; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..265
FT /note="ATP synthase subunit a"
FT /id="PRO_0000362323"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 195..217
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ SEQUENCE 265 AA; 29715 MW; 874E077D8EDDCA41 CRC64;
MAGHTTADYI SHHLTFLTTG QGFWNVHLDT LFFSLVSGVL FLFFFYRTAS KATSGVPGKF
QCLVEMLVEW VDGVVKDNIH GSDVRHQIGS LALTIFCWVF VMNAIDLIPV DFPPQFAELL
GIHYLRAVPT ADISATLGMS VCVFALIIFY TIKSKGLGGF VKEYTLHPFN HWAFIPVNFL
LEAVTLLAKP ISLAFRLFGN MYAGELIFVL IAVMYMADNI IPQVLGIPLH LIWAIFHILV
ITLQAFIFMM LTVVYLSIAY NKSDH
