Y192_ALISL
ID Y192_ALISL Reviewed; 224 AA.
AC B6EPP3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=UPF0758 protein VSAL_I0192;
GN OrderedLocusNames=VSAL_I0192;
OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS LFI1238)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=316275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LFI1238;
RX PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT LFI1238 shows extensive evidence of gene decay.";
RL BMC Genomics 9:616-616(2008).
CC -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR EMBL; FM178379; CAQ77877.1; -; Genomic_DNA.
DR RefSeq; WP_012549070.1; NC_011312.1.
DR AlphaFoldDB; B6EPP3; -.
DR SMR; B6EPP3; -.
DR STRING; 316275.VSAL_I0192; -.
DR EnsemblBacteria; CAQ77877; CAQ77877; VSAL_I0192.
DR KEGG; vsa:VSAL_I0192; -.
DR eggNOG; COG2003; Bacteria.
DR HOGENOM; CLU_073529_0_1_6; -.
DR OMA; AMPDYEL; -.
DR OrthoDB; 1833204at2; -.
DR Proteomes; UP000001730; Chromosome 1.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd08071; MPN_DUF2466; 1.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR025657; RadC_JAB.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR001405; UPF0758.
DR InterPro; IPR020891; UPF0758_CS.
DR PANTHER; PTHR30471; PTHR30471; 1.
DR Pfam; PF04002; RadC; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR TIGRFAMs; TIGR00608; radc; 1.
DR PROSITE; PS50249; MPN; 1.
DR PROSITE; PS01302; UPF0758; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT CHAIN 1..224
FT /note="UPF0758 protein VSAL_I0192"
FT /id="PRO_1000089787"
FT DOMAIN 102..224
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 173..186
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 224 AA; 25341 MW; D56B63BE97219890 CRC64;
MSLMNLPEES RPREKLLALG PKSLTDAELL AIFLRTGIKG MNAIELADKL LKEFGSLRKL
LGSNENEFCS HKGLGTAKFA QLQAVVEMTE RYLFEKIEKE DALTSPEHTK RYLTRILRDR
HREAFYVLFL DNQHRVLKGE VLFEGTIDAA AVYPREVVKR SIDYNAAAII LAHNHPSGVA
EPSQADRRIT KRISDAVELV DIRVLDHFVI GDGEIVSFAE RGWI