HMUV_BURMA
ID HMUV_BURMA Reviewed; 272 AA.
AC Q62A98;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=BMAA1830;
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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; CP000011; AAU45782.1; -; Genomic_DNA.
DR RefSeq; WP_004188492.1; NC_006349.2.
DR RefSeq; YP_106381.1; NC_006349.2.
DR AlphaFoldDB; Q62A98; -.
DR SMR; Q62A98; -.
DR STRING; 243160.BMAA1830; -.
DR EnsemblBacteria; AAU45782; AAU45782; BMAA1830.
DR GeneID; 56596992; -.
DR KEGG; bma:BMAA1830; -.
DR PATRIC; fig|243160.12.peg.5430; -.
DR eggNOG; COG4559; Bacteria.
DR HOGENOM; CLU_000604_1_11_4; -.
DR OMA; KALCQEI; -.
DR Proteomes; UP000006693; Chromosome 2.
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; Translocase; Transport.
FT CHAIN 1..272
FT /note="Hemin import ATP-binding protein HmuV"
FT /id="PRO_0000269582"
FT DOMAIN 2..255
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 272 AA; 28401 MW; 088A93846E628CB0 CRC64;
MLNADHLHVA RDGRAILNDL SIRIAPGCVT ALLGRNGAGK STLLGVLAGD LPAGGLARGA
TVRGGVALNG EPLHAIDAPR LARLRAVLPQ ASRPAFAFSA REIVLLGRYP HARRAGALTH
ADGEIASQAL ALAGATALDA RDVTTLSGGE LARVQFARVL AQLWPPPGAA QPPRYLLLDE
PTAALDLAHQ HQLLDTVRRL SRDWNLGVLT IVHDPNLAAR HADRIAMLAD GAIVAQGAPA
DVLRPEPIAR CYGFRVRLVD AGDGVAPVIV PA
