HMUV_VIBA7
ID HMUV_VIBA7 Reviewed; 260 AA.
AC Q70YG7; F7YI33;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 107.
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=VAA_01383;
OS Vibrio anguillarum (strain ATCC 68554 / 775) (Listonella anguillarum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=882102;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN HEMIN TRANSPORT.
RC STRAIN=ATCC 68554 / 775 / H775-3;
RX PubMed=15342586; DOI=10.1128/jb.186.18.6159-6167.2004;
RA Mourino S., Osorio C.R., Lemos M.L.;
RT "Characterization of heme uptake cluster genes in the fish pathogen Vibrio
RT anguillarum.";
RL J. Bacteriol. 186:6159-6167(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 68554 / 775;
RX PubMed=21576332; DOI=10.1128/iai.05138-11;
RA Naka H., Dias G.M., Thompson C.C., Dubay C., Thompson F.L., Crosa J.H.;
RT "Complete genome sequence of the marine fish pathogen Vibrio anguillarum
RT harboring the pJM1 virulence plasmid and genomic comparison with other
RT virulent strains of V. anguillarum and V. ordalii.";
RL Infect. Immun. 79:2889-2900(2011).
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:15342586}.
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=CAF25489.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ496544; CAF25489.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002284; AEH33069.1; -; Genomic_DNA.
DR RefSeq; WP_013856730.1; NC_015633.1.
DR AlphaFoldDB; Q70YG7; -.
DR SMR; Q70YG7; -.
DR EnsemblBacteria; AEH33069; AEH33069; VAA_01383.
DR KEGG; van:VAA_01383; -.
DR PATRIC; fig|882102.3.peg.1483; -.
DR eggNOG; COG4559; Bacteria.
DR HOGENOM; CLU_000604_1_11_6; -.
DR OMA; KALCQEI; -.
DR Proteomes; UP000006800; Chromosome I.
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 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Translocase; Transport.
FT CHAIN 1..260
FT /note="Hemin import ATP-binding protein HmuV"
FT /id="PRO_0000269635"
FT DOMAIN 7..243
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01718"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01718"
SQ SEQUENCE 260 AA; 28484 MW; DCC0CAA12C8FAE67 CRC64;
MSTTAAIQAS NISVTFGHRT ILDKIDIEIF SGQVTALLGP NGAGKSTLLK ILSGEISSTG
KMAYFGVPQA LWQPNELAKH LAILPQQSTL SFPFIAQEVV ELGALPLNLS HQQVSEVALH
YMQQTDISDR ANNLYPALSG GEKQRLHLAR VLTQLHHSGD KKILMLDEPT SALDLAHQHN
TLRIARSLAH QEQCAVVVVL HDLNLAAQYA DRMVMLHNGK LVCDAPPWEA LNAERIEQVY
GYSSLVAAHP TMDFPMVYPI