ID Q31QX1_SYNE7 Unreviewed; 440 AA.
AC Q31QX1;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=C-terminal processing peptidase-2. Serine peptidase. MEROPS family S41A {ECO:0000313|EMBL:ABB56548.1};
GN OrderedLocusNames=Synpcc7942_0516 {ECO:0000313|EMBL:ABB56548.1};
OS Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS (Anacystis nidulans R2).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1140 {ECO:0000313|EMBL:ABB56548.1, ECO:0000313|Proteomes:UP000889800};
RN [1] {ECO:0000313|Proteomes:UP000889800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805
RC {ECO:0000313|Proteomes:UP000889800};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR EMBL; CP000100; ABB56548.1; -; Genomic_DNA.
DR RefSeq; WP_011243316.1; NZ_JACJTX010000002.1.
DR AlphaFoldDB; Q31QX1; -.
DR STRING; 1140.Synpcc7942_0516; -.
DR MEROPS; S41.009; -.
DR PaxDb; 1140-Synpcc7942_0516; -.
DR GeneID; 76399259; -.
DR KEGG; syf:Synpcc7942_0516; -.
DR eggNOG; COG0793; Bacteria.
DR HOGENOM; CLU_017295_0_0_3; -.
DR OrthoDB; 9812068at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0516-MONOMER; -.
DR Proteomes; UP000889800; Chromosome.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00988; PDZ_CTP_protease; 1.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.750.44; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004404};
KW Protease {ECO:0000256|RuleBase:RU004404};
KW Reference proteome {ECO:0000313|Proteomes:UP000889800};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 108..178
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 388..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 440 AA; 48307 MW; 107F00396BE04143 CRC64;
MSLFSRLRFS VYGSALLAAS GAVCIGISAE HARALPWQDS PKVVLDQAWQ LIDREYVDPT
FNRQDWQAVR RELLSRNYGS NEEAYAALRS ALRRLDDPYT RFLAPEQFKT LTEQTAGEAS
GIGIEIIPDS KDSRPRIQAI LDNSPASKGD VQVGDRILAI DADSTRELTL DEVRNRLQGK
VGSEIDLKLQ RGDRIFSVKL TRVQIEIPSV TAELRQHSGR SVGYIQLREF TAHAAREMRT
SIRSLDEQGA TSYVLDLRGN PGGLLYSSIE IARMWLNNGT IVKTVDRNGK SETINANNSA
ITNKPLAVLV DQNSASSSEI LVGALKDNNR AVVIGRQTFG KALVQSVHTL ADGSGLAVTV
AHYYTPNGTD LGNRGIQPDV EVRLNQRQQA LQRSDPSFLG SNQDPTYGQA IATLEQRTAE
STPSPASSPQ LSQRPSEIRP
//
