ID   HRTA_STAAS              Reviewed;         221 AA.
AC   Q6G6W1;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Putative hemin import ATP-binding protein HrtA;
DE            EC=7.6.2.-;
GN   Name=hrtA; OrderedLocusNames=SAS2250;
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: Part of the ABC transporter complex hrt involved in hemin
CC       import. Responsible for energy coupling to the transport system (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (HrtA),
CC       two transmembrane proteins (HrtB) and a solute-binding protein.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. HrtA family.
CC       {ECO:0000305}.
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DR   EMBL; BX571857; CAG44063.1; -; Genomic_DNA.
DR   RefSeq; WP_001229911.1; NC_002953.3.
DR   AlphaFoldDB; Q6G6W1; -.
DR   SMR; Q6G6W1; -.
DR   KEGG; sas:SAS2250; -.
DR   HOGENOM; CLU_000604_1_22_9; -.
DR   OMA; PTRGHID; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   CDD; cd03255; ABC_MJ0796_LolCDE_FtsE; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017911; MacB_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding; Translocase;
KW   Transport.
FT   CHAIN           1..221
FT                   /note="Putative hemin import ATP-binding protein HrtA"
FT                   /id="PRO_0000270131"
FT   DOMAIN          3..221
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         39..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   221 AA;  24626 MW;  88CE0C08FC09F703 CRC64;
     MALVVEDIVK NFGEGLSETK VLKGINFEVE QGEFVILNGA SGSGKTTLLT ILGGLLSQTS
     GTVLYNDAPL FDKQHRPSDL RLEDIGFIFQ SSHLVPYLKV IEQLTLVGQE AGMTKQQSST
     RAIQLLKNIG LEDRLNVYPH QLSGGEKQRV AIMRAFMNNP KIILADEPTA SLDADRATKV
     VEMIRQQIKE QQMIGIMITH DRRLFEYADR VIELEDGKIT D