ID   PRCA_TRIV2              Reviewed;         662 AA.
AC   P23916; Q3M5X2;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 3.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Calcium-dependent protease;
DE            EC=3.4.21.-;
DE   AltName: Full=Trypsin;
DE   Flags: Precursor;
GN   Name=prcA; OrderedLocusNames=Ava_4009;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-648, AND PROTEIN SEQUENCE OF 192-205
RP   AND 258-262.
RX   PubMed=1900347; DOI=10.1007/bf00282649;
RA   Maldener I., Lockau W., Cai Y., Wolk C.P.;
RT   "Calcium-dependent protease of the cyanobacterium Anabaena: molecular
RT   cloning and expression of the gene in Escherichia coli, sequencing and
RT   site-directed mutagenesis.";
RL   Mol. Gen. Genet. 225:113-120(1991).
RN   [3]
RP   SEQUENCE REVISION, AND SUBCELLULAR LOCATION.
RX   PubMed=8944762; DOI=10.1111/j.1432-1033.1996.00750.x;
RA   Baier K., Nicklisch S., Maldener I., Lockau W.;
RT   "Evidence for propeptide-assisted folding of the calcium-dependent protease
RT   of the cyanobacterium Anabaena.";
RL   Eur. J. Biochem. 241:750-755(1996).
RN   [4]
RP   ERRATUM OF PUBMED:8944762.
RA   Baier K., Nicklisch S., Maldener I., Lockau W.;
RL   Eur. J. Biochem. 245:214-214(1997).
CC   -!- FUNCTION: Degrades phycobiliproteins in vitro. Has a substrate
CC       specificity similar to that of trypsin.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8944762}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA40274.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CP000117; ABA23614.1; -; Genomic_DNA.
DR   EMBL; X56955; CAA40274.1; ALT_FRAME; Genomic_DNA.
DR   PIR; S13335; PRAISB.
DR   AlphaFoldDB; P23916; -.
DR   SMR; P23916; -.
DR   STRING; 240292.Ava_4009; -.
DR   MEROPS; S08.079; -.
DR   EnsemblBacteria; ABA23614; ABA23614; Ava_4009.
DR   KEGG; ava:Ava_4009; -.
DR   eggNOG; COG1404; Bacteria.
DR   eggNOG; COG4935; Bacteria.
DR   HOGENOM; CLU_011263_10_1_3; -.
DR   OMA; LCHPELV; -.
DR   Proteomes; UP000002533; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07498; Peptidases_S8_15; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR002884; P_dom.
DR   InterPro; IPR034054; Pep_S8_PrcA.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cytoplasm; Direct protein sequencing; Hydrolase; Protease;
KW   Serine protease; Zymogen.
FT   PROPEP          1..?
FT                   /id="PRO_0000027132"
FT   CHAIN           ?..662
FT                   /note="Calcium-dependent protease"
FT                   /id="PRO_0000027133"
FT   DOMAIN          196..529
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DOMAIN          535..662
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT   ACT_SITE        233
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        270
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        466
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CONFLICT        610
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   662 AA;  71598 MW;  92BD5B3445299B78 CRC64;
     MVHVRYGGQN GEQYELAISE NHIVVRTESR SSLISDRPFE AAPVSPQARN ILNQFELSTR
     FSQAGVEVLH VKEPSHDGAL RDTAREILNQ EPEVQFAGRV LIDPVSQQPI VYTENLFVKF
     DHEEDVSFCQ EILGRYGLTI KRQLEYARNA YFVSAPSNTG LAIFDISERL LNEESVELCH
     PELVREFRQR QAFPPQWHLK QTTIGGKTIN AHANVEAAWK LSDGTGTIIA IIDDGVDIDH
     EEFRSSGKIV APRDVTRKTN FPTPGNRDNH GTACAGVACG NGNFGASGVA PGAKLMPIRF
     VSALGSQDEA DSFVWAAQNG ADVISCSWGP PDGTWWDDKD PLHKQKVPLP DSTRLAMDYA
     INKGRNGKGC VILFAAGNGN ESVDNDGYAS YEKVIAVAAC NDFGTRSAYS DFGTAVWCAF
     PSNNGNPSQT PGIWTADRTG VVGYNSGNTN LGDQAGNYTN SFGGTSSACP GAAGVAALIL
     SRNPNLRWDE VRDIIKRSCD RIDPVGGNYN AEGRSPFYGY GRINALKAVE LALPAQPEPV
     SIFTAVQDVP INDLQISQLS LAIANTNPIK SIKVTVDIEH TYIGDLVVSL NPPAESGVLP
     IILHDRKGGG ADDIKQTYDE VSTPGLTALK GKIPQGTWTL EVADKAQADT GKIRSLTIEL
     GF