ATPB_LACLM
ID ATPB_LACLM Reviewed; 469 AA.
AC A2RMI2; Q9RAU0;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=ATP synthase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=F-ATPase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
GN Name=atpD {ECO:0000255|HAMAP-Rule:MF_01347}; OrderedLocusNames=llmg_1946;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10940012; DOI=10.1128/jb.182.17.4738-4743.2000;
RA Koebmann B.J., Nilsson D., Kuipers O.P., Jensen P.R.;
RT "The membrane bound H+-ATPase complex is essential for growth of
RT Lactococcus lactis.";
RL J. Bacteriol. 182:4738-4743(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The catalytic sites are hosted primarily by the
CC beta subunits. {ECO:0000255|HAMAP-Rule:MF_01347}.
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_01347};
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_01347}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01347};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01347}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAL98514.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF059739; AAF02210.1; -; Genomic_DNA.
DR EMBL; AM406671; CAL98514.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_014735119.1; NZ_WJVF01000007.1.
DR AlphaFoldDB; A2RMI2; -.
DR SMR; A2RMI2; -.
DR STRING; 416870.llmg_1946; -.
DR EnsemblBacteria; CAL98514; CAL98514; llmg_1946.
DR GeneID; 61110023; -.
DR KEGG; llm:llmg_1946; -.
DR eggNOG; COG0055; Bacteria.
DR HOGENOM; CLU_022398_0_2_9; -.
DR BioCyc; LLAC416870:LLMG_RS09735-MON; -.
DR Proteomes; UP000000364; Chromosome.
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 Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005722; ATP_synth_F1_bsu.
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; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01039; atpD; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis; ATP-binding; Cell membrane; CF(1); Hydrogen ion transport;
KW Ion transport; Membrane; Nucleotide-binding; Translocase; Transport.
FT CHAIN 1..469
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000285241"
FT BINDING 156..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ SEQUENCE 469 AA; 50867 MW; B65CF838CF6F885B CRC64;
MSSGKITQVI GPVVDVEFGS DAKLPEINNA LIVYKDVNGL KTKITLEVAL ELGDGAVRTI
AMESTDGLTR GLEVLDTGKA VSVPVGESTL GRVFNVLGDV IDGGEDFPAD AERNPIHKKA
PTFDELSTAN EVLVTGIKVV DLLAPYLKGG KVGLFGGAGV GKTVLIQELI HNIAQEHGGI
SVFTGVGERT REGNDLYWEM KESGVIEKTA MVFGQMNEPP GARMRVALTG LTIAEYFRDV
QGQDVLLFID NIFRFTQAGS EVSALLGRMP SAVGYQPTLA TEMGQLQERI TSTKKGSVTS
IQAIYVPADD YTDPAPATAF AHLDATTNLE RRLTQMGIYP AVDPLASSSR ALTPEIVGEE
HYEVAMEVQR VLQRYKELQD IIAILGMDEL SDDEKILVGR ARRIQFFLSQ NFHVAEQFTG
QPGSYVPIDK TVHDFKEILE GKYDEVPEDA FRGVGPIEDV LAKAKSMGY
