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Database: UniProt
Entry: B5TKH9_STEMA
LinkDB: B5TKH9_STEMA
Original site: B5TKH9_STEMA 
ID   B5TKH9_STEMA            Unreviewed;       177 AA.
AC   B5TKH9;
DT   04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=H(+)-transporting two-sector ATPase {ECO:0000313|EMBL:ACH90553.1};
DE   Flags: Fragment;
GN   Name=atpD {ECO:0000313|EMBL:ACH90553.1};
OS   Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas
OS   maltophilia).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=40324 {ECO:0000313|EMBL:ACH90553.1};
RN   [1] {ECO:0000313|EMBL:ACH90553.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LMG 10871 {ECO:0000313|EMBL:ACH90553.1};
RX   PubMed=19251858; DOI=10.1128/JB.00892-08;
RA   Kaiser S., Biehler K., Jonas D.;
RT   "A Stenotrophomonas maltophilia multilocus sequence typing scheme for
RT   inferring population structure.";
RL   J. Bacteriol. 191:2934-2943(2009).
RN   [2] {ECO:0000313|EMBL:ADK67103.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LMG 10857 {ECO:0000313|EMBL:ADK67103.1};
RX   PubMed=21247714; DOI=10.1016/j.syapm.2010.11.011;
RA   Vasileuskaya-Schulz Z., Kaiser S., Maier T., Kostrzewa M., Jonas D.;
RT   "Delineation of Stenotrophomonas spp. by multi-locus sequence analysis and
RT   MALDI-TOF mass spectrometry.";
RL   Syst. Appl. Microbiol. 34:35-39(2011).
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936}.
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DR   EMBL; EU983615; ACH90553.1; -; Genomic_DNA.
DR   EMBL; HM370143; ADK67103.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5TKH9; -.
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:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.12240; -; 1.
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   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   CF(1) {ECO:0000256|ARBA:ARBA00023196};
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          57..177
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:ACH90553.1"
FT   NON_TER         177
FT                   /evidence="ECO:0000313|EMBL:ACH90553.1"
SQ   SEQUENCE   177 AA;  19014 MW;  BB657659CCFCDE5D CRC64;
     RAISVPVGAG TLGRIMDVLG RPIDEAGPVA ASDTWEIHRS APSYEDQSPA TELLETGIKV
     IDLMCPFAKG GKVGLFGGAG VGKTVNMMEL INNIAKAHSG LSVFAGVGER TREGNDFYHE
     MKDSNVLDKV AMVYGQMNEP PGNRLRVALT GLTMAEYFRD EKDENGKGKD VLLFVDN
//
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