ID Y2766_STAAR Reviewed; 570 AA.
AC Q6GDC0;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=Putative ABC transporter ATP-binding protein SAR2766;
DE EC=7.-.-.-;
GN OrderedLocusNames=SAR2766;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
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; BX571856; CAG41741.1; -; Genomic_DNA.
DR RefSeq; WP_000138663.1; NC_002952.2.
DR AlphaFoldDB; Q6GDC0; -.
DR SMR; Q6GDC0; -.
DR KEGG; sar:SAR2766; -.
DR HOGENOM; CLU_000604_86_7_9; -.
DR Proteomes; UP000000596; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProt.
DR CDD; cd03225; ABC_cobalt_CbiO_domain1; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR43553:SF29; COBALT IMPORT ATP-BINDING PROTEIN CBIO; 1.
DR PANTHER; PTHR43553; HEAVY METAL TRANSPORTER; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF12558; DUF3744; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 SAR2766"
FT /id="PRO_0000092073"
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; 64206 MW; EBC0DB7E9E37F619 CRC64;
MTEPIISFKD FSFQYHSQAT PTLQNINVDI YPGEKVLVVG ASGSGKSTFA NCINGLIPFK
TKGNVTGELH INNQDATVSC LHKRSNVVGT VLQDTDGQFI GLTAAEDMAF LLENNCVEQD
DMKKNVSYWA EKVDMIEHLN HRPQDLSGGQ KQRVSLGGIL IHRTPILILD EPLANLDPAT
GHETLRLLNN IHEETKSTMI IVEHRLEESL DDTFDRVLLF KDGKIIANTT PSDLLKSSKL
KEAGIREPLY CTALKYAEVD VESIDNLANL REVCMSEHVK FKVKKWIDKT SSNDDNKYKS
EPLLELNEVC VQYSDYSNSV LNNVQLNVYR REMLSIVGHN GAGKSTLAKA ICGFLDITGN
IQFCNKGFNQ LSISERSEFI GYVMQNPNHM ISEKMIYDEV ALGLRARGMK ESDIKIRVEN
VLKICGLYAF RNWPIAALSY GQKKRVTIAS VLVLNPEIII LDEPTAGQDF YHYNEIMSFL
IELNRQGKTI IMITHDMHLL SEYSSRTVVL SKGQVVADTT PVLVLNDKKI CEIASLRQTS
LFEMAEYIGI SEPQKLIQLF INHDRKVRRQ
//
