HMUV_YERPE
ID HMUV_YERPE Reviewed; 266 AA.
AC Q56993; Q0WK27;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
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};
GN OrderedLocusNames=YPO0279, y0539, YP_0434;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN HEMIN TRANSPORT.
RC STRAIN=KIM6;
RX PubMed=10417152; DOI=10.1128/iai.67.8.3879-3892.1999;
RA Thompson J.M., Jones H.A., Perry R.D.;
RT "Molecular characterization of the hemin uptake locus (hmu) from Yersinia
RT pestis and analysis of hmu mutants for hemin and hemoprotein utilization.";
RL Infect. Immun. 67:3879-3892(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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:10417152}.
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 -!- INTERACTION:
CC Q56993; Q56992: hmuU; NbExp=3; IntAct=EBI-2866017, EBI-16023192;
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=AAM84127.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U60647; AAC64870.1; -; Genomic_DNA.
DR EMBL; AL590842; CAL18965.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM84127.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS60705.1; -; Genomic_DNA.
DR PIR; AC0035; AC0035.
DR PIR; T12073; T12073.
DR RefSeq; WP_002209058.1; NZ_WHLN01000017.1.
DR RefSeq; YP_002345361.1; NC_003143.1.
DR PDB; 4G1U; X-ray; 3.01 A; C/D=1-266.
DR PDBsum; 4G1U; -.
DR AlphaFoldDB; Q56993; -.
DR SMR; Q56993; -.
DR DIP; DIP-60001N; -.
DR IntAct; Q56993; 3.
DR STRING; 214092.YPO0279; -.
DR TCDB; 3.A.1.14.5; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q56993; -.
DR EnsemblBacteria; AAM84127; AAM84127; y0539.
DR EnsemblBacteria; AAS60705; AAS60705; YP_0434.
DR GeneID; 66843247; -.
DR KEGG; ype:YPO0279; -.
DR KEGG; ypk:y0539; -.
DR KEGG; ypm:YP_0434; -.
DR PATRIC; fig|1028802.3.peg.940; -.
DR eggNOG; COG4559; Bacteria.
DR HOGENOM; CLU_000604_1_11_6; -.
DR OMA; KALCQEI; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
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 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..266
FT /note="Hemin import ATP-binding protein HmuV"
FT /id="PRO_0000092392"
FT DOMAIN 12..248
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01718"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01718"
FT STRAND 11..21
FT /evidence="ECO:0007829|PDB:4G1U"
FT STRAND 24..35
FT /evidence="ECO:0007829|PDB:4G1U"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:4G1U"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:4G1U"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:4G1U"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:4G1U"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:4G1U"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:4G1U"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:4G1U"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:4G1U"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:4G1U"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:4G1U"
FT TURN 133..136
FT /evidence="ECO:0007829|PDB:4G1U"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:4G1U"
FT HELIX 144..158
FT /evidence="ECO:0007829|PDB:4G1U"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:4G1U"
FT HELIX 180..196
FT /evidence="ECO:0007829|PDB:4G1U"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:4G1U"
FT HELIX 208..214
FT /evidence="ECO:0007829|PDB:4G1U"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:4G1U"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:4G1U"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:4G1U"
FT HELIX 238..244
FT /evidence="ECO:0007829|PDB:4G1U"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:4G1U"
FT STRAND 255..264
FT /evidence="ECO:0007829|PDB:4G1U"
SQ SEQUENCE 266 AA; 29658 MW; 4A7DEB955583CB27 CRC64;
MVDMAVTPVA LLEASHLHYH VQQQALINDV SLHIASGEMV AIIGPNGAGK STLLRLLTGY
LSPSHGECHL LGQNLNSWQP KALARTRAVM RQYSELAFPF SVSEVIQMGR APYGGSQDRQ
ALQQVMAQTD CLALAQRDYR VLSGGEQQRV QLARVLAQLW QPQPTPRWLF LDEPTSALDL
YHQQHTLRLL RQLTRQEPLA VCCVLHDLNL AALYADRIML LAQGKLVACG TPEEVLNAET
LTQWYQADLG VSRHPESALP QIYLRQ
