ID   HMUV_SALRD              Reviewed;         273 AA.
AC   Q2RZ08;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 108.
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}; OrderedLocusNames=SRU_2731;
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC   Rhodothermaceae; Salinibacter.
OX   NCBI_TaxID=309807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / CECT 5946 / M31;
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA   Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA   Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA   Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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 inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01718}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       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; CP000159; ABC46293.1; -; Genomic_DNA.
DR   RefSeq; WP_011405435.1; NC_007677.1.
DR   RefSeq; YP_446823.1; NC_007677.1.
DR   AlphaFoldDB; Q2RZ08; -.
DR   SMR; Q2RZ08; -.
DR   STRING; 309807.SRU_2731; -.
DR   EnsemblBacteria; ABC46293; ABC46293; SRU_2731.
DR   GeneID; 61497514; -.
DR   KEGG; sru:SRU_2731; -.
DR   eggNOG; COG4559; Bacteria.
DR   HOGENOM; CLU_000604_1_11_10; -.
DR   OMA; KALCQEI; -.
DR   Proteomes; UP000008674; 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; 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.
DR   PROSITE; PS51261; HMUV; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..273
FT                   /note="Hemin import ATP-binding protein HmuV"
FT                   /id="PRO_0000269625"
FT   DOMAIN          2..242
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01718"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01718"
SQ   SEQUENCE   273 AA;  28721 MW;  98125A57EF95CF1B CRC64;
     MIALRDITVH IGDATLIERV SAAVRPGQMT AVVGPNGAGK TTLLRVASGE LTPSEGAVQL
     DDRPLAALSE QAQARRRAVL PQASRLHFAF SVLEVVLMGR TPHVQGREGP EDWAIAEDAL
     DAVAMAGFAD RDVPTLSGGE QQRVHLARAL AQIWTPPDDG HRYLLLDEPT ASLDLAHQQN
     VLRTARAFAD QGAGVLAILH DLNLAAQFAD HVVVMADGGV HAQGAPASVL TPPCIREVFG
     WPVCVLAHPT QSCPLIVPDG AEAGATVSDP NSL