ID   HMUV_RHOJR              Reviewed;         292 AA.
AC   Q0SIB7;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Hemin import ATP-binding protein HmuV {ECO:0000255|HAMAP-Rule:MF_01718};
DE            EC=7.6.2.- {ECO:0000255|HAMAP-Rule:MF_01718};
GN   Name=hmuV {ECO:0000255|HAMAP-Rule:MF_01718};
GN   OrderedLocusNames=RHA1_ro00886;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- FUNCTION: Part of the ABC transporter complex HmuTUV involved in hemin
CC       import. Responsible for energy coupling to the transport system.
CC       {ECO:0000255|HAMAP-Rule:MF_01718}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (HmuV),
CC       two transmembrane proteins (HmuU) and a solute-binding protein (HmuT).
CC       {ECO:0000255|HAMAP-Rule:MF_01718}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01718};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01718}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Heme (hemin)
CC       importer (TC 3.A.1.14.5) family. {ECO:0000255|HAMAP-Rule:MF_01718}.
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DR   EMBL; CP000431; ABG92719.1; -; Genomic_DNA.
DR   RefSeq; WP_011594104.1; NC_008268.1.
DR   AlphaFoldDB; Q0SIB7; -.
DR   SMR; Q0SIB7; -.
DR   STRING; 101510.RHA1_ro00886; -.
DR   EnsemblBacteria; ABG92719; ABG92719; RHA1_ro00886.
DR   KEGG; rha:RHA1_ro00886; -.
DR   PATRIC; fig|101510.16.peg.907; -.
DR   eggNOG; COG4559; Bacteria.
DR   HOGENOM; CLU_000604_1_11_11; -.
DR   OMA; RYAWNGL; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51261; HMUV; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..292
FT                   /note="Hemin import ATP-binding protein HmuV"
FT                   /id="PRO_0000269623"
FT   DOMAIN          38..271
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01718"
FT   BINDING         70..77
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01718"
SQ   SEQUENCE   292 AA;  31376 MW;  1AF9FA23AAF0D15D CRC64;
     MSPAFHPLRT RVGEAIEQSL FRRTDPVPPP RPSGAVTLRA DGIAVTRGGR PVLDDVSVDV
     RIGEVLVLVG PNGAGKSTLL AALSGDQDVH TGTVHLDDRD LGEWTALEMA QRRAVLPQQN
     TVGFSFTARQ VITMGRSPWA RTPRSDDDAV AIAEAMRICD VVAFADRPFT ALSGGERARV
     ALARVLAQRT ETILLDEPTA ALDLGHQETV MRLARSRAEQ GTAVVVVLHD LALAAAYADR
     IVVLEQGRVA ANGPPADVLS EELLTRVYGH PVEVIEHPVT GATLVLPRRD QR