HMUV_SHIDY
ID HMUV_SHIDY Reviewed; 256 AA.
AC O70014;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=shuV;
OS Shigella dysenteriae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=622;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O-4576;
RX PubMed=9393841; DOI=10.1128/iai.65.12.5358-5363.1997;
RA Mills M., Payne S.M.;
RT "Identification of shuA, the gene encoding the heme receptor of Shigella
RT dysenteriae, and analysis of invasion and intracellular multiplication of a
RT shuA mutant.";
RL Infect. Immun. 65:5358-5363(1997).
RN [2]
RP FUNCTION IN HEMIN TRANSPORT.
RC STRAIN=O-4576;
RX PubMed=7768795; DOI=10.1128/jb.177.11.3004-3009.1995;
RA Mills M., Payne S.M.;
RT "Genetics and regulation of heme iron transport in Shigella dysenteriae and
RT detection of an analogous system in Escherichia coli O157:H7.";
RL J. Bacteriol. 177:3004-3009(1995).
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:7768795}.
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; U64516; AAC27811.1; -; Genomic_DNA.
DR RefSeq; WP_005019012.1; NZ_QWTT01000105.1.
DR AlphaFoldDB; O70014; -.
DR SMR; O70014; -.
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 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Translocase; Transport.
FT CHAIN 1..256
FT /note="Hemin import ATP-binding protein HmuV"
FT /id="PRO_0000269628"
FT DOMAIN 2..238
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 256 AA; 28954 MW; 1A19D13B53E719D8 CRC64;
MISAQNLVYS LQGRRLTDNV SLTFPGGEIV AILGPNGAGK STLLRQLTGY LQPDSGECRL
FNKPLNEWSI TELAKHRAVM RQNSHMAFPF SVQEVIQMGR HPHRTGNQDN ETAQIMALCD
CQALANRDYR QLSGGEQQRV QLARLLVQLW EPTPSPKWLF LDEPTSALDI HHQQHLFRLL
RQLVHERQFN VCCVLHDLNL AARYADRIVL MQKGKVIANG KPQDVLTQQE LTMLYGADIT
VLEDPANHSP LIVLDH