ID A0A1Z4J8W3_LEPBY Unreviewed; 392 AA.
AC A0A1Z4J8W3;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Peptidase S1 and S6 chymotrypsin/Hap {ECO:0000313|EMBL:BAY53205.1};
GN ORFNames=NIES2135_00070 {ECO:0000313|EMBL:BAY53205.1};
OS Leptolyngbya boryana NIES-2135.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1973484 {ECO:0000313|EMBL:BAY53205.1, ECO:0000313|Proteomes:UP000217895};
RN [1] {ECO:0000313|EMBL:BAY53205.1, ECO:0000313|Proteomes:UP000217895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2135 {ECO:0000313|EMBL:BAY53205.1,
RC ECO:0000313|Proteomes:UP000217895};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; AP018203; BAY53205.1; -; Genomic_DNA.
DR RefSeq; WP_017290761.1; NZ_AP018203.1.
DR AlphaFoldDB; A0A1Z4J8W3; -.
DR Proteomes; UP000217895; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR048172; HhoA_HhoB_HtrA-like.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR NCBIfam; NF041521; HhoA_HhoB_HtrA; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000217895};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..392
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011112299"
FT DOMAIN 295..349
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 30..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 392 AA; 41139 MW; EA4FE34E4E8D9903 CRC64;
MASIIKPPLV SLTLILASLS TGCVRNLSAP QEQTVTPQAQ SSNTPVPTPS NPPVANSGGN
PNYVAQVVEQ VGPAVVRVNS TRTLQQPTND PYLRRFFGEQ SPTQQRVQRG TGSGFIISQD
GRILTNAHVV DNADTVSIVL KDGRRFDAKV LGSDRVTDVA VLKIETTGLP TARLGNSDNL
QPGQAAIAIG NPLGLDNTVT EGIVSATGRS SSDVGVPAER VRFIQTDAAI NPGNSGGPLL
NANGEVIGIN TAIIQGAQGI GFAIPINTAQ QVAEQLITKG QVTHPYLGVL MTDLTPELRD
QINRSNVGFQ VNQTTGVLIV RVAENSPAAR AGLRPGDVLI SINGNAVQNT EQVQKTIEGA
QLNNPLPMTV QRNDRSVAVN VRPTQLPPPD AS
//
