HMUV_PSET1
ID HMUV_PSET1 Reviewed; 261 AA.
AC Q3ICT8;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=PSHAb0066;
OS Pseudoalteromonas translucida (strain TAC 125).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=326442;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAC 125;
RX PubMed=16169927; DOI=10.1101/gr.4126905;
RA Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT Pseudoalteromonas haloplanktis TAC125.";
RL Genome Res. 15:1325-1335(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; CR954247; CAI89116.1; -; Genomic_DNA.
DR RefSeq; WP_011329708.1; NC_007482.1.
DR AlphaFoldDB; Q3ICT8; -.
DR SMR; Q3ICT8; -.
DR STRING; 326442.PSHAb0066; -.
DR EnsemblBacteria; CAI89116; CAI89116; PSHAb0066.
DR KEGG; pha:PSHAb0066; -.
DR PATRIC; fig|326442.8.peg.2981; -.
DR eggNOG; COG4559; Bacteria.
DR HOGENOM; CLU_000604_1_11_6; -.
DR OMA; RYAWNGL; -.
DR OrthoDB; 1752365at2; -.
DR BioCyc; PHAL326442:PSHA_RS15185-MON; -.
DR Proteomes; UP000006843; Chromosome II.
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..261
FT /note="Hemin import ATP-binding protein HmuV"
FT /id="PRO_0000269611"
FT DOMAIN 2..243
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 261 AA; 28686 MW; BD5BFCED630A8B5C CRC64;
MLCANNVSAQ IGQKKLLKHI NFYVKPNELV VIIGPNGAGK SSLLKALCGD IKINNGDITL
NDRLLSDYSI ASLATLRAVL TQNYELDFPF SVAEVVDMAH FAHQADYSKQ QLMHFSEQVM
QALSVTHLKT HTFTQLSGGE KQRVQLARVL CQIQPSLVAN KTPYLLIDEP TSSLDIFHQY
DVMAQAKSIA SQGAGVVAVI HDLSLAASFA DRIYMLNNGE VAACGIPKEV LTPALLKRVY
NINARLENNT SEAMPHIQMC Y