ID B4XBC3_XANCI Unreviewed; 249 AA.
AC B4XBC3; A0A0N7AJ51;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=ATP synthase beta chain {ECO:0000313|EMBL:AJE69099.1};
DE SubName: Full=F1-F0-ATPase beta subunit {ECO:0000313|EMBL:ABW82257.1};
DE Flags: Fragment;
GN Name=atpD {ECO:0000313|EMBL:ABW82257.1};
OS Xanthomonas citri pv. vignicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=473426 {ECO:0000313|EMBL:ABW82257.1};
RN [1] {ECO:0000313|EMBL:ABW82257.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LMG 8139 {ECO:0000313|EMBL:ABW82257.1}, and LMG 828
RC {ECO:0000313|EMBL:ABW82258.1};
RX PubMed=19196770; DOI=10.1099/ijs.0.65453-0;
RA Ah-You N., Gagnevin L., Grimont P.A., Brisse S., Nesme X., Chiroleu F.,
RA Bui Thi Ngoc L., Jouen E., Lefeuvre P., Verniere C., Pruvost O.;
RT "Polyphasic characterization of xanthomonads pathogenic to members of the
RT Anacardiaceae and their relatedness to species of Xanthomonas.";
RL Int. J. Syst. Evol. Microbiol. 59:306-318(2009).
RN [2] {ECO:0000313|EMBL:AJE69099.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LMG 8136 {ECO:0000313|EMBL:AJE69099.1}, and LMG 828
RC {ECO:0000313|EMBL:AJE69101.1};
RA Madsen J.;
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AJE69099.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LMG 8136 {ECO:0000313|EMBL:AJE69099.1}, and LMG 828
RC {ECO:0000313|EMBL:AJE69101.1};
RA Constantin E.C., Cleenwreck I., Maes M., Baeyen S., Van Malderghem C.,
RA De Vos P., Cottyn B.;
RT "Genetic characterization of strains named as Xanthomonas axonopodis pv.
RT dieffenbachiae leads to a taxonomic revision of the X. axonopodis species
RT complex.";
RL Plant Pathol. 0:0-0(2015).
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. T3SS ATPase
CC subfamily. {ECO:0000256|ARBA:ARBA00024342}.
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DR EMBL; EU015199; ABW82257.1; -; Genomic_DNA.
DR EMBL; EU015200; ABW82258.1; -; Genomic_DNA.
DR EMBL; KJ491162; AJE69099.1; -; Genomic_DNA.
DR EMBL; KJ491164; AJE69101.1; -; Genomic_DNA.
DR AlphaFoldDB; B4XBC3; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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-KW.
DR GO; GO:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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 PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 3..50
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 108..248
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABW82257.1"
FT NON_TER 249
FT /evidence="ECO:0000313|EMBL:ABW82257.1"
SQ SEQUENCE 249 AA; 26741 MW; 640E9DAC14120620 CRC64;
NEVPKVYHAL KVDGTEITLE VQQQLGDGVV RTIALGSTDG LKRNLVATNT ERAISVPVGA
GTLGRIMDVL GRPIDEAGDV QASDHWEIHR GAPSYEDQSS STELLETGIK VIDLMCPFAK
GGKVGLFGGA GVGKTVNMME LINNIAKAHS GLSVFAGVGE RTREGNDFYH EMKDSNVLDK
VAMVYGQMNE PPGNRLRVAL TGLTMAEYFR DEKDASGKGK DVLLFVDNIY RYTLAGTEVS
ALLGRMPSA
//
