HMUV_CUPMC
ID HMUV_CUPMC Reviewed; 261 AA.
AC Q1LC89;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=Rmet_5378;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OG Plasmid megaplasmid.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
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; CP000353; ABF12237.1; -; Genomic_DNA.
DR RefSeq; WP_011519784.1; NC_007974.2.
DR AlphaFoldDB; Q1LC89; -.
DR SMR; Q1LC89; -.
DR STRING; 266264.Rmet_5378; -.
DR EnsemblBacteria; ABF12237; ABF12237; Rmet_5378.
DR KEGG; rme:Rmet_5378; -.
DR eggNOG; COG4559; Bacteria.
DR HOGENOM; CLU_000604_1_11_4; -.
DR OMA; HHADRVW; -.
DR OrthoDB; 1752365at2; -.
DR Proteomes; UP000002429; Plasmid megaplasmid CH34.
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 inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Plasmid; Reference proteome; Translocase; Transport.
FT CHAIN 1..261
FT /note="Hemin import ATP-binding protein HmuV"
FT /id="PRO_0000269614"
FT DOMAIN 2..243
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 261 AA; 27585 MW; AEF048EFA86E2810 CRC64;
MLIARNLSCS RGRRQILSGI DLTLPAGEMV GVLGANGAGK STLLGTLAGE LPGDDAAVSL
CNRPLTDWPV DELARSRAVL PQSPGLGFDL GVTEVVAMGG YPFPEMGKHT LDTLLDRALA
LADVAHLATR SYQSLSGGEQ QRVQFARALV QVLACRTADS YRALLLDEPI SSLDPRHQLQ
LLGTARNLCH TDALAVLVVL HDVNLAARWC DRLVLLADGR TVASGTPADV LTPPNLATVY
GIPATVMESP VHRGVPMVVF G
