ATPB_CORGL
ID ATPB_CORGL Reviewed; 483 AA.
AC P42464;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 154.
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};
GN OrderedLocusNames=Cgl1212, cg1368;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX PubMed=8085791; DOI=10.1007/bf00873088;
RA Ludwig W., Neumaier J., Klugbauer N., Brockmann E., Roller C.,
RA Klugbauer S., Reetz K., Schachtner I., Ludvigsen A., Bachleitner M.,
RA Fischer U., Schleifer K.H.;
RT "Phylogenetic relationships of Bacteria based on comparative sequence
RT analysis of elongation factor Tu and ATP-synthase beta-subunit genes.";
RL Antonie Van Leeuwenhoek 64:285-305(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14067 / DSM 20411 / NCIB 9565 / 2247;
RA Sekine H., Tomita F., Yokota A.;
RT "Nucleotide sequence of atp operon of Brevibacterium flavum.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13060 / LMG 3653 / NCIB 10333 / 614;
RA Sekine H., Yokota A., Tomita F.;
RT "Nucleotide sequence of atp operon of Corynebacterium glutamicum.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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}.
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DR EMBL; X76875; CAA54202.1; -; Genomic_DNA.
DR EMBL; AB048368; BAB13360.1; -; Genomic_DNA.
DR EMBL; AB046112; BAB08157.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98605.1; -; Genomic_DNA.
DR EMBL; BX927151; CAF19916.1; -; Genomic_DNA.
DR PIR; I40716; I40716.
DR RefSeq; NP_600437.1; NC_003450.3.
DR RefSeq; WP_011014204.1; NC_003450.3.
DR AlphaFoldDB; P42464; -.
DR SMR; P42464; -.
DR STRING; 196627.cg1368; -.
DR World-2DPAGE; 0001:P42464; -.
DR KEGG; cgb:cg1368; -.
DR KEGG; cgl:Cgl1212; -.
DR PATRIC; fig|196627.13.peg.1191; -.
DR eggNOG; COG0055; Bacteria.
DR HOGENOM; CLU_022398_0_2_11; -.
DR OMA; GFNMIMD; -.
DR Proteomes; UP000000582; 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; Reference proteome;
KW Translocase; Transport.
FT CHAIN 1..483
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000144435"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT CONFLICT 461
FT /note="D -> E (in Ref. 1; CAA54202, 2; BAB13360, 3;
FT BAB08157 and 5; CAF19916)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 52538 MW; DF0A3932D1D170A8 CRC64;
MTTALEEQNA QQAATAGRVV RVIGAVVDVE FPRGELPALY NALTVEVTLE SVKKTVVLEV
AQHLGDNLIR TIAMAPTDGL VRGAAVTDTA RPISVPVGDV VKGHVFNALG DCLDDVSLNN
NPEIERWGIH REPPSFDQLE GKTEILETGI KVIDLLTPYV KGGKIGLFGG AGVGKTVLIQ
EMITRIAREF SGTSVFAGVG ERTREGTDLF LEMEEMGVLQ DTALVFGQMD EPPGVRMRVA
LSGLTMAEYF RDVQNQDVLL FIDNIFRFTQ AGSEVSTLLG RMPSAVGYQP TLADEMGVLQ
ERITSTKGRS ITSLQAVYVP ADDYTDPAPA TTFAHLDATT ELDRSIASKG IYPAVNPLTS
TSRILEPAIV GERHYEVSQR VIGILQKNKE LQDIIAILGM DELSEEDKIT VARARRIERF
LGQNFFVAEK FTGLPGSYVP LTDTVDAFER ICNGDFDHYP DQAFNGLGGL DDVEAAYKKL
TGK
