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ATP6_STAEQ
ID   ATP6_STAEQ              Reviewed;         242 AA.
AC   Q5HMB3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, 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=SERP1715;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01393};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-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; CP000029; AAW55108.1; -; Genomic_DNA.
DR   RefSeq; WP_001829936.1; NC_002976.3.
DR   AlphaFoldDB; Q5HMB3; -.
DR   SMR; Q5HMB3; -.
DR   STRING; 176279.SERP1715; -.
DR   EnsemblBacteria; AAW55108; AAW55108; SERP1715.
DR   GeneID; 50018193; -.
DR   KEGG; ser:SERP1715; -.
DR   eggNOG; COG0356; Bacteria.
DR   HOGENOM; CLU_041018_2_3_9; -.
DR   OMA; FTHAVRL; -.
DR   OrthoDB; 867266at2; -.
DR   Proteomes; UP000000531; Chromosome.
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 membrane; CF(0); Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..242
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_1000145318"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        118..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ   SEQUENCE   242 AA;  27343 MW;  1C9B697AF68378E1 CRC64;
     MDHKSPLVSW NVFGFDIVFN LASVLMVVIT AILVFILAIV CTRNLKKRPT GKQNFIEWVF
     DFVRGIIESN MAWKKGGNFH FLAVTLILFI FVANMLGLPF AIVTHDHTLW WKSPTADATV
     TLTLSTTMIL LTHYYGIKMR GTKAYAAGYF KPFWPLAIIN VFEEFTSTLT LGLRLYGNIF
     AGELLLGLLA SLFFEQPAWG WIISIPGLIV WQAFSIFVGT IQAYIFVMLS MVYMSHKVAD
     GH
 
 
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