Y2708_STAAC
ID Y2708_STAAC Reviewed; 570 AA.
AC Q5HCL3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Putative ABC transporter ATP-binding protein SACOL2708;
DE EC=7.-.-.-;
GN OrderedLocusNames=SACOL2708;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW37356.1; -; Genomic_DNA.
DR RefSeq; WP_000138655.1; NC_002951.2.
DR AlphaFoldDB; Q5HCL3; -.
DR SMR; Q5HCL3; -.
DR PRIDE; Q5HCL3; -.
DR EnsemblBacteria; AAW37356; AAW37356; SACOL2708.
DR KEGG; sac:SACOL2708; -.
DR HOGENOM; CLU_000604_86_7_9; -.
DR OMA; DPMTRLD; -.
DR Proteomes; UP000000530; Chromosome.
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 SACOL2708"
FT /id="PRO_0000092064"
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; 64144 MW; F4DDE3E4457F8C6C CRC64;
MTEPIISFKD FSFQYHSQAT PTLQNINVDI 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 RNWPIAALSY GQKKRVTIAS VLVLNPEIII LDEPTAGQDF YHYNEIMSFL
IELNRQGKTI IMITHDMHLL SEYSSRTVVL SKGQVVADTT PVLVLNDKKI CEIASLRQTS
LFEMAEYIGI SEPQKLVQLF INHDRKVRRQ