ID D5BKK0_ZUNPS Unreviewed; 465 AA.
AC D5BKK0;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Periplasmic trypsin-like serine protease {ECO:0000313|EMBL:ADF53912.1};
GN OrderedLocusNames=ZPR_3597 {ECO:0000313|EMBL:ADF53912.1};
OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87) (Wangia
OS profunda).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zunongwangia.
OX NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF53912.1, ECO:0000313|Proteomes:UP000001654};
RN [1] {ECO:0000313|EMBL:ADF53912.1, ECO:0000313|Proteomes:UP000001654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87
RC {ECO:0000313|Proteomes:UP000001654};
RX PubMed=20398413; DOI=10.1186/1471-2164-11-247;
RA Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., Dang H.Y.,
RA Zhou B.C., Yu J., Zhang Y.Z.;
RT "The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation
RT to the deep-sea environment and ecological role in sedimentary organic
RT nitrogen degradation.";
RL BMC Genomics 11:247-247(2010).
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DR EMBL; CP001650; ADF53912.1; -; Genomic_DNA.
DR RefSeq; WP_013072996.1; NC_014041.1.
DR AlphaFoldDB; D5BKK0; -.
DR STRING; 655815.ZPR_3597; -.
DR MEROPS; S01.453; -.
DR KEGG; zpr:ZPR_3597; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_10; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000001654; 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; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ADF53912.1}.
FT DOMAIN 270..361
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 465 AA; 50380 MW; 0EE5E0EFEB6DCF21 CRC64;
MRKLASLLIV SILGGALTLG SYKLFFEEEN VSFLQEKQDA TQSLIQANYD ANRTYGTNVD
FTAAAEKTVH AVVHVKNVAV YSGPRSWADV MQGKTESSKA LRGTGSGVII TPDGYIVTNN
HVIDGANELE VTLNNNKTYK AKVIGTDAIS DIALIKVEPE EDLEYIPFGN SNNTKVGEWV
LAVGNPFNLK STVTAGIISA KSRNLNPNAT GQSFIQTDAA INPGNSGGAL VNINGELIGI
NTAITSMTGS YVGYAFAVPS NNARKIVEDI MEYGDIQQGI LGIRGSDFNR TPELSEEYGT
TQGVYVSEVT SGSGAEKAGI KAKDVIRKID NIKVNKFSDL TGYINTKRPN DTVNVTVLRN
GVEKEIAVKL TKLSVTQLPI GLEVTNASKD ELKFYQTENG VKISKTLSDQ YAEEEFVGAI
ITEINGDKIY DIRDAEEAFK SLERGQGLTM TFIDKTGQKQ RVIFR
//
