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ATP6_YERPN
ID   ATP6_YERPN              Reviewed;         274 AA.
AC   Q1CCG9; D1Q307;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=YPN_3984;
GN   ORFNames=YP516_4520;
OS   Yersinia pestis bv. Antiqua (strain Nepal516).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=377628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RA   Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA   Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA   Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT   "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP000305; ABG20311.1; -; Genomic_DNA.
DR   EMBL; ACNQ01000019; EEO74910.1; -; Genomic_DNA.
DR   RefSeq; WP_002228150.1; NZ_ACNQ01000019.1.
DR   AlphaFoldDB; Q1CCG9; -.
DR   SMR; Q1CCG9; -.
DR   EnsemblBacteria; ABG20311; ABG20311; YPN_3984.
DR   GeneID; 66843611; -.
DR   KEGG; ypn:YPN_3984; -.
DR   HOGENOM; CLU_041018_1_0_6; -.
DR   OMA; FTHAVRL; -.
DR   Proteomes; UP000008936; 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 inner membrane; Cell membrane; CF(0);
KW   Hydrogen ion transport; Ion transport; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..274
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000362517"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ   SEQUENCE   274 AA;  30411 MW;  7C3FE57D5A4290E6 CRC64;
     MSASGEISTP RDYIGHHLNH LQLDLRTFEL VNPHSTGPAT FWTLNIDSLF FSVVLGLAFL
     LVFRKVAASA TSGVPGKLQT AVELIIGFVD NSVRDMYHGK SKVIAPLALT VFVWVLLMNM
     MDLLPIDLLP YIGEHVFGLP ALRVVPTADV SITLSMALGV FILIIFYSIK MKGVGGFTKE
     LTMQPFNHPI FIPVNLILEG VSLLSKPLSL GLRLFGNMYA GELIFILIAG LLPWWSQWML
     SVPWAIFHIL IITLQAFIFM VLTIVYLSMA SEEH
 
 
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