ID   HMUV_YEREN              Reviewed;         266 AA.
AC   P74981;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 2.
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}; Synonyms=hemV;
OS   Yersinia enterocolitica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN HEMIN TRANSPORT.
RC   STRAIN=ATCC 51872 / WA-C / Serotype O:8;
RX   PubMed=7997183; DOI=10.1111/j.1365-2958.1994.tb00465.x;
RA   Stojiljkovic I., Hantke K.;
RT   "Transport of haemin across the cytoplasmic membrane through a haemin-
RT   specific periplasmic binding-protein-dependent transport system in Yersinia
RT   enterocolitica.";
RL   Mol. Microbiol. 13:719-732(1994).
CC   -!- FUNCTION: Part of the ABC transporter complex HmuTUV involved in hemin
CC       import. Responsible for energy coupling to the transport system
CC       (Probable). {ECO:0000305|PubMed:7997183}.
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; X77867; CAA54864.1; -; Genomic_DNA.
DR   PIR; S54440; S54440.
DR   RefSeq; WP_005175609.1; NZ_NWMR01000018.1.
DR   AlphaFoldDB; P74981; -.
DR   SMR; P74981; -.
DR   STRING; 1443113.LC20_04861; -.
DR   eggNOG; COG4559; Bacteria.
DR   OrthoDB; 1752365at2; -.
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   1: Evidence at protein level;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..266
FT                   /note="Hemin import ATP-binding protein HmuV"
FT                   /id="PRO_0000269640"
FT   DOMAIN          12..248
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01718"
FT   BINDING         44..51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01718"
SQ   SEQUENCE   266 AA;  29495 MW;  7F606FF07A126BEE CRC64;
     MVDTAVVDTA LLEANQLSYH VQGQKLINNV SLQIASGEMV AIIGPNGAGK STLLRLLTGY
     LAPSEGHCQL LGKNLNSWQP QALARTRAVM RQYSDLAFPF SVSEVIQMGR APYGAAQNRQ
     ALQEVMAQTD CLALAQRDYR ALSGGEQQRV QLARVLAQLW QPEPTSRWLF LDEPTSALDL
     YHQQHTLRLL RQLTLEEPLA VCCVLHDLNL AALYADRILL LAQGELVACG TPEEVLNAET
     LTRWYQADLG ISRHPESALP QIYLRQ