ID A0A1X1QLZ0_9GAMM Unreviewed; 431 AA.
AC A0A1X1QLZ0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:ORU92104.1};
GN ORFNames=A6F72_04030 {ECO:0000313|EMBL:ORU92104.1};
OS Cycloclasticus sp. symbiont of Poecilosclerida sp. N.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Cycloclasticus.
OX NCBI_TaxID=1840472 {ECO:0000313|EMBL:ORU92104.1, ECO:0000313|Proteomes:UP000193416};
RN [1] {ECO:0000313|EMBL:ORU92104.1, ECO:0000313|Proteomes:UP000193416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Specimen N {ECO:0000313|EMBL:ORU92104.1};
RA Rubin Blum M., Dubilier N.;
RT "Short-chain alkanes fuel the metabolism of mussel and sponge
RT Cycloclasticus symbionts from deep-sea gas and oil seeps.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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:ORU92104.1}.
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DR EMBL; LWTM01000074; ORU92104.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1QLZ0; -.
DR STRING; 1840472.A6F72_04030; -.
DR Proteomes; UP000193416; Unassembled WGS sequence.
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 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 NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF03572; Peptidase_S41; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000193416};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 90..158
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 394..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 431 AA; 46567 MW; 20E6B84B1817D07D CRC64;
MNFLHKTLPV LLIGALLGIM VSVGGSILAE KEHVKGSLPL DDLKAFSEVF GQIKASYVEE
VSDHDLLESA IEGMLAGLDP HSTYLDEKDF KDLREGTRGE FGGLGIEVGM EDGFVKVITP
IDDTPAFEAG VEAGDLVIRL NEKPVKGMSL ADAVKIMRGK PGTDIVLTII REGEPKPLKI
SITRAVIKVV SVKNRMLEPG YGYVRIASFQ TRTGANFNDA LSQLKKENEN DELKGLVLDL
RNNPGGLLKA AVAVSDAFLD KGLIVYTEGR IQHSKMRFKA NPNDALNGAP IVVLVNGGSA
SASEIVAGAL QDHKRAVIMG QQSFGKGSVQ TVLENGRGGA IKLTTARYFT PSGRSIQAEG
ITPDVILLKV KLEKLDEDED FVFIKEKDLT KHLENADAEE SAAEKPEKRS SDDYPLNAAL
NLLKGINILR K
//
