ID A0A0A2WI83_9GAMM Unreviewed; 601 AA.
AC A0A0A2WI83;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Carboxyl-terminal protease {ECO:0000313|EMBL:KGQ17965.1};
GN ORFNames=LF41_1819 {ECO:0000313|EMBL:KGQ17965.1};
OS Lysobacter dokdonensis DS-58.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1300345 {ECO:0000313|EMBL:KGQ17965.1, ECO:0000313|Proteomes:UP000030518};
RN [1] {ECO:0000313|EMBL:KGQ17965.1, ECO:0000313|Proteomes:UP000030518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-58 {ECO:0000313|EMBL:KGQ17965.1,
RC ECO:0000313|Proteomes:UP000030518};
RA Kim J.F., Kwak M.-J.;
RT "Genome sequences of Lysobacter dokdonensis DS-58.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGQ17965.1}.
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DR EMBL; JRKJ01000023; KGQ17965.1; -; Genomic_DNA.
DR RefSeq; WP_036171372.1; NZ_JRKJ01000023.1.
DR AlphaFoldDB; A0A0A2WI83; -.
DR STRING; 1300345.LF41_1819; -.
DR PATRIC; fig|1300345.3.peg.2866; -.
DR eggNOG; COG0793; Bacteria.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000030518; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.750.44; -; 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; IPR040573; TSP_N.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR PANTHER; PTHR32060:SF32; TAIL-SPECIFIC PROTEASE; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW Protease {ECO:0000313|EMBL:KGQ17965.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030518};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..601
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001996296"
FT DOMAIN 241..318
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT DOMAIN 319..533
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|SMART:SM00245"
SQ SEQUENCE 601 AA; 64243 MW; B2C26F4481460D1B CRC64;
MVNRFGAVSA LSLVLACSAA LAQVPEEKTF DPGMAIRMVH GLVSDTRFDY FAGRPQEGRA
QRLFDLWIET FDPNAMYAST ADLAPLQDRR DALLQVAKKE DFAAALSLAD AMKALAIARL
EAAKSGIDAA IADKAADDWS ARTADSPRAP DAAALDVLWA RKLRHQVRDL RKTGQQDAQV
RDVLRRYYDA AATRIRGLGS DDIIEGFIDA YANAVDPDAD FMPPPRATDM AELKQSKWSD
LGIGLVLRSD GLETRVESAL PGSAAHFAGI ARGDRLLEIA DGPGGAFVDV FGEPLDKTIE
RLRGPAGSKV RMRLQDSDGL IRVVDVGRAK SPTNPLGYET EQSTLHLDGK TIGVLRPGSL
YVDWDARARK QPDYASASRD VHRLLGEMQA AGVDAVVLDL RNNGGGALSE GIDMAGAFAG
KRTMVLIHEQ GGRTSNEVAK VDAAWDGPLV VLVDRGTASG AELIAAALQD HGRAVIAGEP
TYGRGTIQSL IDLDRWPSPG TKRMGQLKMT IAAMYRVNGA TLEQGVEPDV AFASTQPREP
RTRHVLVGPR ISTKVDIARP VVDRARFAGQ RPLPAATPSQ TDPTLGAAAA LAAEIAAAVS
R
//
