HMUV_VIBCH
ID HMUV_VIBCH Reviewed; 259 AA.
AC Q9KL34; O52047;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 116.
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}; Synonyms=hutD;
GN OrderedLocusNames=VC_A0915;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Classical CA401;
RA Occhino D.O., Payne S.M.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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=AAF96812.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF016580; AAB94549.1; -; Genomic_DNA.
DR EMBL; AE003853; AAF96812.1; ALT_FRAME; Genomic_DNA.
DR PIR; G82400; G82400.
DR RefSeq; WP_001193094.1; NZ_LT906615.1.
DR AlphaFoldDB; Q9KL34; -.
DR SMR; Q9KL34; -.
DR STRING; 243277.VC_A0915; -.
DR DNASU; 2612894; -.
DR EnsemblBacteria; AAF96812; AAF96812; VC_A0915.
DR GeneID; 57742284; -.
DR KEGG; vch:VC_A0915; -.
DR eggNOG; COG4559; Bacteria.
DR HOGENOM; CLU_000604_1_11_6; -.
DR OMA; KALCQEI; -.
DR Proteomes; UP000000584; 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..259
FT /note="Hemin import ATP-binding protein HmuV"
FT /id="PRO_0000269634"
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 259 AA; 28419 MW; FEC3A206D93EFFC7 CRC64;
MQTIAIQGRD LCVTYGSRQV LDHVDITLRC GEVAALLGPN GAGKSTLLKL LCGEMSGAGK
LDYFGVPASQ WPAEKLANHL GILPQQSSLT FPFTAQEVVE LGAIPLNLPR KEVERVARHY
MLKTDVLHLA ASLYPSLSGG EKQRLHLARV LTQLHQAGQQ RILMLDEPTS ALDLAHQHNT
LQLARQLADE EQCAVVVVLH DLNLAAQYSD RLILLHQGKI VCDAAPWQAL TAERIEQVYG
YQALVAAHPT RDFPMVYPA