ID   HMUV_RHOPS              Reviewed;         261 AA.
AC   Q138A9;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=RPD_2348;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000283; ABE39580.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q138A9; -.
DR   SMR; Q138A9; -.
DR   STRING; 316057.RPD_2348; -.
DR   EnsemblBacteria; ABE39580; ABE39580; RPD_2348.
DR   KEGG; rpd:RPD_2348; -.
DR   eggNOG; COG4559; Bacteria.
DR   HOGENOM; CLU_000604_1_11_5; -.
DR   OMA; YPRITWI; -.
DR   OrthoDB; 1752365at2; -.
DR   BioCyc; RPAL316057:RPD_RS11780-MON; -.
DR   Proteomes; UP000001818; 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; Translocase; Transport.
FT   CHAIN           1..261
FT                   /note="Hemin import ATP-binding protein HmuV"
FT                   /id="PRO_0000277706"
FT   DOMAIN          5..241
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01718"
FT   BINDING         37..44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01718"
SQ   SEQUENCE   261 AA;  28343 MW;  7A746D4388565DE5 CRC64;
     MSAALTANAA SFAIGSVALV ERVDLRVEPG ELIAIVGPNG AGKSTLLRML SGDVRPTAGA
     VRMANRDLST YSPRELAGRR AVLAQHTNVG FPFSVEEIVW MGADIDRRKA APLFDRAIRE
     VRLEAFRHRD VTTLSGGEQQ RTHFARVLLQ LWCGEASYGP GLLLLDEPTS SLDIRHQLDL
     AEMARRCARD GTTVIAILHD LNLAARFADR ILMMHQGALT ADGTPSAVIR PDLLARVFDV
     DLSVSRDSTG APFVLPQLAK R