ATPA_PSYWF
ID ATPA_PSYWF Reviewed; 514 AA.
AC A5WBV9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=ATP synthase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01346};
DE AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE AltName: Full=F-ATPase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
GN Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346};
GN OrderedLocusNames=PsycPRwf_0191;
OS Psychrobacter sp. (strain PRwf-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=349106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRwf-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The alpha chain is a regulatory subunit.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01346};
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_01346}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01346}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01346}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
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DR EMBL; CP000713; ABQ93150.1; -; Genomic_DNA.
DR RefSeq; WP_011959484.1; NC_009524.1.
DR AlphaFoldDB; A5WBV9; -.
DR SMR; A5WBV9; -.
DR STRING; 349106.PsycPRwf_0191; -.
DR PRIDE; A5WBV9; -.
DR EnsemblBacteria; ABQ93150; ABQ93150; PsycPRwf_0191.
DR KEGG; prw:PsycPRwf_0191; -.
DR eggNOG; COG0056; Bacteria.
DR HOGENOM; CLU_010091_2_1_6; -.
DR OMA; LQAPGVM; -.
DR OrthoDB; 837522at2; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR CDD; cd01132; F1_ATPase_alpha; 1.
DR Gene3D; 1.20.150.20; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR038376; ATP_synth_asu_C_sf.
DR InterPro; IPR033732; ATP_synth_F1_a.
DR InterPro; IPR005294; ATP_synth_F1_asu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00962; atpA; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis; ATP-binding; Cell inner membrane; Cell membrane; CF(1);
KW Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW Translocase; Transport.
FT CHAIN 1..514
FT /note="ATP synthase subunit alpha"
FT /id="PRO_1000073358"
FT BINDING 170..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 374
FT /note="Required for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ SEQUENCE 514 AA; 55810 MW; EA0A2B569CBB72C4 CRC64;
MQQLNPAEIS QLIKQRIQDL DTSATAKNEG TIVKVSDGIV QIHGLEDAMY GEMIEFEGDV
YGMALNLEQD SVGAVVLGDY LGLQEGQKAY CTGRILEVPV GPELLGRVVD ALGNPIDGKG
PINAKLTDKV EKIAPGVIAR QSVDEPVMTG YKAVDTMIPI GRGQRELIIG DRQTGKTAMA
IDAIIAQKNS GIKCVYVAIG QKRSTIANVV RKLEETGALA YTTVVVASAS EPAALQYIAP
YSGCTMGEYF RDRGEDALIV YDDLSKQAVA YRQISLLLRR PPGREAYPGD VFYLHSRLLE
RASRVNAAYV EEFTNGEVKG QTGSLTALPI IETQAGDVSA FVPTNVISIT DGQIFLESSL
FNSGIRPAVN AGISVSRVGG AAQTKIIKKL SGGIRTALAQ YRELAAFAQF ASDLDDATKQ
QLDHGERVTE LMKQKQYQPM SIAEQAAVIF ASNEGYLSAI PVEKIGAWEE AYLRYMYDEQ
ADLMQEINDT ANYNDDIAGR LKSSVETFLQ NHTF
