HMUV_VIBPA
ID HMUV_VIBPA Reviewed; 260 AA.
AC Q87J32;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 111.
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=VPA0421;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC61764.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000032; BAC61764.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_799931.2; NC_004605.1.
DR RefSeq; WP_005491112.1; NC_004605.1.
DR AlphaFoldDB; Q87J32; -.
DR SMR; Q87J32; -.
DR STRING; 223926.28808587; -.
DR EnsemblBacteria; BAC61764; BAC61764; BAC61764.
DR GeneID; 1191109; -.
DR KEGG; vpa:VPA0421; -.
DR PATRIC; fig|223926.6.peg.3362; -.
DR eggNOG; COG4559; Bacteria.
DR HOGENOM; CLU_000604_1_11_6; -.
DR OMA; KALCQEI; -.
DR Proteomes; UP000002493; 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; 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..260
FT /note="Hemin import ATP-binding protein HmuV"
FT /id="PRO_0000269637"
FT DOMAIN 6..242
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01718"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01718"
SQ SEQUENCE 260 AA; 28765 MW; FB83A2ED77F39F2A CRC64;
MNHVVLSGRN ISMKYGHRLV LDDISIDIRA GEVTALLGPN GAGKSTLLKL LCGEVPSHNE
IDYFGEPKEA WKPEEIAKHL AMLPQHSTLT FPFLAREVVE LGAIPLSLSN KETTELALHY
MQKTDVLHLA ESLYPALSGG EKQRLHLARV LTQLHQSGDK KILMLDEPTS ALDLAHQHNT
LKIAREAAKA QNAAVVVVLH DLNLASQYAD RLVLLHNGKL VCDDNPWQAL TPERIEQVYG
YRSIVTKHPT LDFPQVHAAA
