ID K9V331_9CYAN Unreviewed; 572 AA.
AC K9V331;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:AFZ02099.1};
GN ORFNames=Cal6303_3156 {ECO:0000313|EMBL:AFZ02099.1};
OS Calothrix sp. PCC 6303.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFZ02099.1, ECO:0000313|Proteomes:UP000010477};
RN [1] {ECO:0000313|EMBL:AFZ02099.1, ECO:0000313|Proteomes:UP000010477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6303 {ECO:0000313|EMBL:AFZ02099.1,
RC ECO:0000313|Proteomes:UP000010477};
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; CP003610; AFZ02099.1; -; Genomic_DNA.
DR RefSeq; WP_015198728.1; NC_019751.1.
DR AlphaFoldDB; K9V331; -.
DR STRING; 1170562.Cal6303_3156; -.
DR KEGG; calt:Cal6303_3156; -.
DR PATRIC; fig|1170562.3.peg.3447; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_513607_0_0_3; -.
DR OrthoDB; 500593at2; -.
DR Proteomes; UP000010477; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00306; Peptidases_S8_S53; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000010477};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 145..383
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 154
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 199
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 365
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 572 AA; 62656 MW; 143FD700C48E5054 CRC64;
MEANQSQISP NPETSRFEGF FLQMVTPGLE NECREIVEKV LGADWQVKSI GDNSTEFEIS
LRDDALSSKD AWDKSYNMRS QPGVIDAEPL FAVPVADIKP DLDLSRELFS DEIAKESGDV
TWGLQQMRVL DVWQKYFPDP NKLPGHGIVI GHPDTGYTQH PEVINNLLLD KGFNYIKRTK
DPLDTLETSG GEIINNPGHG TSTASLIISP PGAQGNYANG KYVTGVAPGA KVLPLRVTYS
VVLLSTRSLA EAIEYATDNG CHVITISLGT GLPNRRLRSA ILYAQKRGVI IVAASGTMIP
YVVYPAAYDE VIAVTGSNIR REIWGGASRG KKVDVTAPGQ ALWHAKTRKE NGELTYNIEQ
DSGTSFSAPL VAGVAALWLS YHGRDQLIER YGAENIPSIF NQLLRDSCEK FPTWKPNKFG
AGIVNAEKLL ATPLPDNVNN SFISSALALQ QHSPVDSGEI ETFEHLFESQ IPTSNSISKM
SKLNSSLAQL LQTDENHLPE KLKQVGKELA FHFATNPELY QEFVSALQDE EETVAQGLLG
TQLESPGNKS LSNILLQQGV SNVLHDQLSR EN
//
