ID   HRTA_STAAE              Reviewed;         221 AA.
AC   A6QJK1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Putative hemin import ATP-binding protein HrtA;
DE            EC=7.6.2.-;
GN   Name=hrtA; OrderedLocusNames=NWMN_2261;
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Newman;
RX   PubMed=17951380; DOI=10.1128/jb.01000-07;
RA   Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT   "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT   analysis of staphylococcal genomes: polymorphism and evolution of two major
RT   pathogenicity islands.";
RL   J. Bacteriol. 190:300-310(2008).
RN   [2]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=16933993; DOI=10.1371/journal.ppat.0020087;
RA   Friedman D.B., Stauff D.L., Pishchany G., Whitwell C.W., Torres V.J.,
RA   Skaar E.P.;
RT   "Staphylococcus aureus redirects central metabolism to increase iron
RT   availability.";
RL   PLoS Pathog. 2:777-789(2006).
CC   -!- FUNCTION: Part of the ABC transporter complex hrt involved in hemin
CC       import. Responsible for energy coupling to the transport system
CC       (Probable). {ECO:0000305|PubMed:16933993}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (HrtA),
CC       two transmembrane proteins (HrtB) and a solute-binding protein.
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Highly induced by hemin. {ECO:0000269|PubMed:16933993}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. HrtA family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP009351; BAF68533.1; -; Genomic_DNA.
DR   RefSeq; WP_001229911.1; NZ_CP023390.1.
DR   AlphaFoldDB; A6QJK1; -.
DR   SMR; A6QJK1; -.
DR   EnsemblBacteria; BAF68533; BAF68533; NWMN_2261.
DR   KEGG; sae:NWMN_2261; -.
DR   HOGENOM; CLU_000604_1_22_9; -.
DR   OMA; PTRGHID; -.
DR   Proteomes; UP000006386; Chromosome.
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   2: Evidence at transcript level;
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_0000317035"
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