ID   ATP6_PSEPU              Reviewed;         153 AA.
AC   P25761;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   02-MAR-2010, entry version 64.
DE   RecName: Full=ATP synthase subunit a;
DE   AltName: Full=F-ATPase subunit 6;
DE   AltName: Full=ATP synthase F0 sector subunit a;
DE   Flags: Fragment;
GN   Name=atpB; Synonyms=uncB;
OS   Pseudomonas putida.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TN2100;
RX   MEDLINE=92204018; PubMed=1552862;
RX   DOI=10.1111/j.1365-2958.1992.tb01510.x;
RA   Ogasawara N., Yoshikawa H.;
RT   "Genes and their organization in the replication origin region of the
RT   bacterial chromosome.";
RL   Mol. Microbiol. 6:629-634(1992).
CC   -!- FUNCTION: Key component of the proton channel; it plays a direct
CC       role in the translocation of protons across the membrane (By
CC       similarity).
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC       has three main subunits: a(1), b(2) and c(9-12). The alpha and
CC       beta chains form an alternating ring which encloses part of the
CC       gamma chain. CF(1) is attached to CF(0) by a central stalk formed
CC       by the gamma and epsilon chains, while a peripheral stalk is
CC       formed by the delta and b chains (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the ATPase A chain family.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X62540; CAA44424.1; -; Genomic_DNA.
DR   PIR; JQ1226; JQ1226.
DR   BRENDA; 3.6.3.14; 403.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, c...; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:hydrogen ion transporting ATP synthase acti...; IEA:HAMAP.
DR   GO; GO:0042777; P:plasma membrane ATP synthesis coupled proto...; IEA:HAMAP.
DR   HAMAP; MF_01393; ATP_synth_a_bact; 1; -.
DR   InterPro; IPR000568; ATPase_F0-cplx_asu.
DR   Pfam; PF00119; ATP-synt_A; 1.
DR   SUPFAM; SSF81336; ATPase_F0_A; 1.
DR   PROSITE; PS00449; ATPASE_A; PARTIAL.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell inner membrane; Cell membrane; CF(0);
KW   Hydrogen ion transport; Ion transport; Membrane; Transmembrane;
KW   Transport.
FT   CHAIN         1   >153       ATP synthase subunit a.
FT                                /FTId=PRO_0000082066.
FT   TRANSMEM     43     63       Potential.
FT   TRANSMEM    104    124       Potential.
FT   NON_TER     153    153
SQ   SEQUENCE   153 AA;  16607 MW;  7CBCF4E7CB4E47B1 CRC64;
     MAAETASGYI QHHLQNLTYG QLPDGSWGFA HSAAEAKAMG FWAFHLDTLG WSVALGLIFL
     LIFRMAAKKA TSGQPGGLQN FVEVMVDFVN GSVKDSFHGR SPVIAPLALT IFVWVFLMNA
     VDLIPVDWIP QLAILISGDP HIPFRAVSTT DPN
//