HMUV_SHIDS
ID HMUV_SHIDS Reviewed; 256 AA.
AC Q32AY3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
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}; Synonyms=shuV;
GN OrderedLocusNames=SDY_3547;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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}.
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DR EMBL; CP000034; ABB63522.1; -; Genomic_DNA.
DR RefSeq; WP_001626196.1; NC_007606.1.
DR RefSeq; YP_405013.1; NC_007606.1.
DR AlphaFoldDB; Q32AY3; -.
DR SMR; Q32AY3; -.
DR STRING; 300267.SDY_3547; -.
DR TCDB; 3.A.1.14.18; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; ABB63522; ABB63522; SDY_3547.
DR KEGG; sdy:SDY_3547; -.
DR PATRIC; fig|300267.13.peg.4209; -.
DR HOGENOM; CLU_000604_1_11_6; -.
DR OMA; KALCQEI; -.
DR Proteomes; UP000002716; 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 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..256
FT /note="Hemin import ATP-binding protein HmuV"
FT /id="PRO_0000269627"
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; 28896 MW; 1A19D57B17E719D8 CRC64;
MISAQNLVYS LQGRRLTDNV SLTFPGGEIV AILGPNGAGK STLLRQLTGY LQPDSGECRL
FNKPLNEWSI TELAKHRAVM RQNSHMAFPF SVQEVIQMGR HPHRTGNQDN ETAQIMALCD
CQALANRDYR QLSGGEQQRV QLARLLVQLW EPTPSPKWLF LDEPTSALDI HHQQHLFRLL
RQLVHERQFN VCCVLHDLNL AARYADRIVL MQKGKVIANG KPQDVLTQQA LTMLYGADIT
VLEDPANHSP LIVLDH
