Y1534_SYNY3
ID Y1534_SYNY3 Reviewed; 301 AA.
AC P74220;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Putative carboxypeptidase slr1534;
DE EC=3.4.16.-;
GN OrderedLocusNames=slr1534;
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 -!- SIMILARITY: Belongs to the peptidase S66 family. {ECO:0000305}.
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DR EMBL; BA000022; BAA18314.1; -; Genomic_DNA.
DR PIR; S75855; S75855.
DR AlphaFoldDB; P74220; -.
DR SMR; P74220; -.
DR IntAct; P74220; 1.
DR STRING; 1148.1653400; -.
DR MEROPS; S66.001; -.
DR PaxDb; P74220; -.
DR EnsemblBacteria; BAA18314; BAA18314; BAA18314.
DR KEGG; syn:slr1534; -.
DR eggNOG; COG1619; Bacteria.
DR InParanoid; P74220; -.
DR OMA; MLTQWRL; -.
DR PhylomeDB; P74220; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10740; -; 1.
DR Gene3D; 3.50.30.60; -; 1.
DR InterPro; IPR027461; Carboxypeptidase_A_C_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR027478; LdcA_N.
DR InterPro; IPR040449; Peptidase_S66_N.
DR InterPro; IPR040921; Peptidase_S66C.
DR InterPro; IPR003507; S66_fam.
DR PANTHER; PTHR30237; PTHR30237; 1.
DR Pfam; PF02016; Peptidase_S66; 1.
DR Pfam; PF17676; Peptidase_S66C; 1.
DR PIRSF; PIRSF028757; LD-carboxypeptidase; 1.
DR SUPFAM; SSF141986; SSF141986; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase; Hydrolase; Protease; Reference proteome; Serine protease.
FT CHAIN 1..301
FT /note="Putative carboxypeptidase slr1534"
FT /id="PRO_0000172846"
FT ACT_SITE 116
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 276
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 301 AA; 32906 MW; 18D9F11762CA95D8 CRC64;
MSSLPKNFLQ PLPLQPGDRL TVVSPSGSLR ELADLQKGVD IWRSWGYEVI FSQGYHNRFG
YLAGTDQQRR QDLLHAWLDP QCKGILCSRG GYGSARLLED WQWPAISQPK WVLGFSDVTG
ILWSLLKSGI ISLHGPVLTT LSDEPDWALE RLRGHLQGLP LAPLTGNSWQ KGMARGRLVA
GNLTVATHFL GTEWQPDFEN VILAIEDVTE SPYRIDRMVT QWRASGNLSQ VAGIALGRFS
ECEAPAGFPS WTVEEVLGDR LGDLGIPVVA DLPFGHGGVN AILPVGSKAE LDGDAGTLSF
L