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ATP6_PSECP
ID   ATP6_PSECP              Reviewed;         266 AA.
AC   B8HAZ5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=Achl_2344;
OS   Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP
OS   107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS   chlorophenolicus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Pseudarthrobacter.
OX   NCBI_TaxID=452863;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 / NCIMB
RC   13794 / A6;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.;
RT   "Complete sequence of chromosome of Arthrobacter chlorophenolicus A6.";
RL   Submitted (JAN-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 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; CP001341; ACL40309.1; -; Genomic_DNA.
DR   RefSeq; WP_015937521.1; NC_011886.1.
DR   AlphaFoldDB; B8HAZ5; -.
DR   SMR; B8HAZ5; -.
DR   STRING; 452863.Achl_2344; -.
DR   EnsemblBacteria; ACL40309; ACL40309; Achl_2344.
DR   KEGG; ach:Achl_2344; -.
DR   eggNOG; COG0356; Bacteria.
DR   HOGENOM; CLU_041018_0_1_11; -.
DR   OMA; FTHAVRL; -.
DR   OrthoDB; 867266at2; -.
DR   Proteomes; UP000002505; 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; IPR000568; ATP_synth_F0_asu.
DR   InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR   InterPro; IPR035908; F0_ATP_A_sf.
DR   PANTHER; PTHR11410; PTHR11410; 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.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW   Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..266
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_1000184276"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        191..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ   SEQUENCE   266 AA;  28967 MW;  1F168D4EF2E6BCEB CRC64;
     MIALALPAQD SGEFTPPGIN EMHLPAILPW GAAEGFSKQM LLVLLSVVFI AVFFVLAARK
     QQLVPGKLQF AGEAAYGFVR NGIAKDIIGG RDFIKYVPLL FSLFFFILVN NIYGAIPLIQ
     LPTFSHVGGA YVLAGIVYFT WIAIGIKKNG LRYFKLATVP SGVPWFILPI VIPIEIISNF
     VVRPVTHSLR LFATMLAGHL IVMIAGSGIE YLVMQESILL KGTSVLVLAG AIAMYMLEAL
     IMVLQAYVFT LLTAIYIEGA LHADSH
 
 
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