Y1821_SYNY3
ID Y1821_SYNY3 Reviewed; 366 AA.
AC P73714;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Putative zinc metalloprotease slr1821;
DE EC=3.4.24.-;
GN OrderedLocusNames=slr1821;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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; BA000022; BAA17761.1; -; Genomic_DNA.
DR PIR; S77203; S77203.
DR AlphaFoldDB; P73714; -.
DR SMR; P73714; -.
DR IntAct; P73714; 4.
DR STRING; 1148.1652842; -.
DR PaxDb; P73714; -.
DR EnsemblBacteria; BAA17761; BAA17761; BAA17761.
DR KEGG; syn:slr1821; -.
DR eggNOG; COG0750; Bacteria.
DR InParanoid; P73714; -.
DR OMA; QYMVGFG; -.
DR PhylomeDB; P73714; -.
DR BRENDA; 3.4.24.85; 6192.
DR Proteomes; UP000001425; 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; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837; PTHR42837; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR TIGRFAMs; TIGR00054; TIGR00054; 2.
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..366
FT /note="Putative zinc metalloprotease slr1821"
FT /id="PRO_0000088472"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 106..188
FT /note="PDZ"
FT ACT_SITE 21
FT /evidence="ECO:0000255"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 366 AA; 38982 MW; CCB373F5089255D6 CRC64;
MSVLAALAAI GVLAVLIAVH ELGHFAAARL QGIHVTRFAL GFGPPLLKYQ GAETEYSIRA
IPLGGYVAFP DDDPDSEIPA DDPNLLKNRP ILDRAIVISA GVIANLVFAY FLLIGQVSTI
GFQNIQPGLV IPQVDSASAA QVAGMEPGDI VLSLQGNTLP GFPDATTQFI DIVRRSPSVP
ITVEVQRGEE TKTLTITPTP DAEGKGKIGV ALLPNVETKR ASNPLEALTY SAEAFERIVK
LTTQGFWQLI SNFADNASQV AGPVKIVEYG ANIARSDASN LFQFGALISI NLAVINILPL
PALDGGQLVF LLIEGLLGKP LPEKFQMGVM QTGLVLLLSL GVFLIVRDTL NLTFVQEFLP
SFTGYE
