Y1411_RALSO
ID Y1411_RALSO Reviewed; 462 AA.
AC Q8XZI4;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Putative zinc metalloprotease RSc1411;
DE EC=3.4.24.-;
GN OrderedLocusNames=RSc1411; ORFNames=RS05281;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR EMBL; AL646052; CAD15113.1; -; Genomic_DNA.
DR RefSeq; WP_011001360.1; NC_003295.1.
DR AlphaFoldDB; Q8XZI4; -.
DR SMR; Q8XZI4; -.
DR STRING; 267608.RSc1411; -.
DR EnsemblBacteria; CAD15113; CAD15113; RSc1411.
DR GeneID; 60500934; -.
DR KEGG; rso:RSc1411; -.
DR PATRIC; fig|267608.8.peg.1442; -.
DR eggNOG; COG0750; Bacteria.
DR HOGENOM; CLU_025778_0_1_4; -.
DR OMA; QYMVGFG; -.
DR Proteomes; UP000001436; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837; PTHR42837; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 2.
DR TIGRFAMs; TIGR00054; TIGR00054; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..462
FT /note="Putative zinc metalloprotease RSc1411"
FT /id="PRO_0000088454"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 201..283
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 462 AA; 49614 MW; 3F2818F8B0C1121B CRC64;
MLTVLAFVFA IAVLIVVHEL GHYSVARLCG VKVLRFSVGF GKVLFRRVGR GPDRTEWTLC
AIPLGGYVKM LGESARDPER DPPIPPEDLP RTFDHQPVYK RFAIVAAGPV FNFLLAIALY
ALLAWVGAQE PLPILGAPPP GSIAAQADLR AKDRVVAVGT DEEAPTPVRA WSDVRMRLYE
AGIGGRDAIV QVRGADGAER TVRLRELPSA ARSPQVDVIE QVGLRLLGGP VTIAEVLPGS
AGERAGLRRG DQIVRFAGQP ADQASDLIRW IRAMPEQNAS IDILRDGLPM TLPVRLGADA
DSANPGGPKL GKLGAQLSQH VETELIRDEP VHALGHAMRE VWRTSMLSLK VLGKMIVGQA
SLQNLSGPIT VADFAGKAAS LGWQSFVAFL ALISVSLGVL NLLPVPVLDG GHLLYYCVEF
LTGKPVPESW QAVLQKIGIA CILLLTSLAL YNDLSRLFLA HG