ID A0A249SVE6_9BACT Unreviewed; 710 AA.
AC A0A249SVE6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Tail-specific protease {ECO:0000313|EMBL:ASZ11569.1};
GN ORFNames=CK934_11670 {ECO:0000313|EMBL:ASZ11569.1};
OS Chitinophaga sp. MD30.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=2033437 {ECO:0000313|EMBL:ASZ11569.1, ECO:0000313|Proteomes:UP000217148};
RN [1] {ECO:0000313|EMBL:ASZ11569.1, ECO:0000313|Proteomes:UP000217148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD30 {ECO:0000313|EMBL:ASZ11569.1,
RC ECO:0000313|Proteomes:UP000217148};
RA Wan X., Darris M., Hou S., Donachie S.P.;
RT "Draft genome sequence of a novel Chitinophaga sp., MD30, isolated from a
RT biofilm in an air conditioner condensate pipe.";
RL Submitted (AUG-2017) 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; CP023254; ASZ11569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A249SVE6; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000217148; 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 InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR InterPro; IPR020992; Tail_Prtase_C.
DR InterPro; IPR040573; TSP_N.
DR NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR PANTHER; PTHR32060:SF32; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF11818; DUF3340; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF17804; TSP_NTD; 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; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004404};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:ASZ11569.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217148};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..710
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012331977"
FT DOMAIN 247..335
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 710 AA; 79144 MW; 4E768A2401A73283 CRC64;
MKVIIPALLL TISAGVLAFS KLGHADDPPG KYEVIMNLVG QVLKEGHYQP KPIDDAFSKA
VFTKYLKDLD SEKKFFLKKD VDSLDALSTH IDDELKGAPV ECFTAINGVI KRRIAEAAAI
YPAILNQPFD FTKDDKVVLD PDKLDYPGSE DARKDAWYKV LKYRTLEKLT DLQDIRDKEK
EKAKAGTTPK TDVQLEVEAR AKVKQIYDRY FDRLKNKQDD NERFSMYVNA ITTTMDPHTD
FFPPVEKRYF EEQMSGKFFG IGAQLREEDG KIKIVSIVTG SPSWKQGQLK ANDVIIKVAE
KGKEPLDITG YAVDDAVKVI RGAKGSTVIL TVRSVDGTVK DVPIVRDEIV LDETFAKSAI
IQGKHKIGYI YLPEFYADFQ DRNGARSGDD VAKEIQKLKA EQVEGIILDL RFNGGGSLQD
VVQMAGLFIP EGPVVQVRSR GGENVVLRDR DKNVQYDGPL AIMVNEFSAS ASEIMAAAMQ
DYKRAVIIGS PTTYGKGTVQ RMLNLDDLLP GKLADLGSLG ALKLTVQKFY RANGGSTQLK
GVSSDIVLPD PYYEVAERKD KDALAWDEIP KASYTPWHSP VNVDALKKNS TQRVNSSEAF
KMVNENINTL KSIEKKESYS LNMQTFKAEQ KANAAALKKY DVANEKIKEL SISNLKIDLD
KLGADSAKIA RNKDWIKFRS KDIYLDEAVN VMNDLINMSG PHLNNKAGNR
//
