Y2569_STAAS
ID Y2569_STAAS Reviewed; 570 AA.
AC Q6G5Z1;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Putative ABC transporter ATP-binding protein SAS2569;
DE EC=7.-.-.-;
GN OrderedLocusNames=SAS2569;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC -!- FUNCTION: Probably part of an ABC transporter complex. Responsible for
CC energy coupling to the transport system (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; BX571857; CAG44386.1; -; Genomic_DNA.
DR RefSeq; WP_000138645.1; NC_002953.3.
DR AlphaFoldDB; Q6G5Z1; -.
DR SMR; Q6G5Z1; -.
DR KEGG; sas:SAS2569; -.
DR HOGENOM; CLU_000604_86_7_9; -.
DR OMA; DPMTRLD; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProt.
DR CDD; cd03225; ABC_cobalt_CbiO_domain1; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR022216; ABC_Co_transporter.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR015856; ABC_transpr_CbiO/EcfA_su.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF12558; DUF3744; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding; Repeat;
KW Translocase; Transport.
FT CHAIN 1..570
FT /note="Putative ABC transporter ATP-binding protein
FT SAS2569"
FT /id="PRO_0000092076"
FT DOMAIN 6..247
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 304..537
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 338..345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 570 AA; 64187 MW; E65782B56486F1F7 CRC64;
MTEPIISFKD FSFQYHSQAT PTLQKINVDI YPGEKVLVVG ASGSGKSTFA NCINGLIPFK
TKGNITGELY INNQDATVSC LHDRSNVVGT VLQDTDGQFI GLTAAEDMAF LLENNCVEQD
DMKKNVSYWA EKVGMIEHLN HRPQDLSGGQ KQRVSLGGIL IHRTPILILD EPLANLDPAT
GHETLRLLNN IHEETKSTMI IVEHRLEESL DDTFDRVLLF KDGKIIANTT PSDLLKSSKL
KEAGIREPLY CTALKYAEVD VESIDNLANL RDVCMSEHVK FKVKKWIDET SANNDNKYKS
EPLLELNEVC VQYSDYSNSV LNNVQLNVYR REMLSIVGHN GAGKSTLAKA ICGFLDITGN
IQFCNRGFNQ LSISERSEFV GYVMQNPNHM ISEKMIYDEV ALGLRARGMK ESDIKIRVEN
VLKICGLYAF RNWPIVALSY GQKKRVTIAS VLVLNPEIII LDEPTAGQDF YHYNEIMSFL
IELNRQGKTI IMITHDMHLL SEYSSRTVVL SKGQVVADTT PVLVLNDKKI CEIASLRQTS
LFEMAEYIGI SEPQKLVQLF INHDRKVRRQ