ID I4VQG5_9GAMM Unreviewed; 754 AA.
AC I4VQG5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=C-terminal processing peptidase {ECO:0000313|EMBL:EIL89456.1};
GN ORFNames=UU5_15748 {ECO:0000313|EMBL:EIL89456.1};
OS Rhodanobacter sp. 115.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1162282 {ECO:0000313|EMBL:EIL89456.1, ECO:0000313|Proteomes:UP000004557};
RN [1] {ECO:0000313|EMBL:EIL89456.1, ECO:0000313|Proteomes:UP000004557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=115 {ECO:0000313|EMBL:EIL89456.1,
RC ECO:0000313|Proteomes:UP000004557};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
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:EIL89456.1}.
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DR EMBL; AJXS01000377; EIL89456.1; -; Genomic_DNA.
DR RefSeq; WP_008214834.1; NZ_AJXS01000377.1.
DR AlphaFoldDB; I4VQG5; -.
DR MEROPS; S41.001; -.
DR PATRIC; fig|1162282.3.peg.2971; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000004557; 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 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:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 3, CHLOROPLASTIC; 1.
DR PANTHER; PTHR32060; 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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004404};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004404};
KW Serine protease {ECO:0000256|RuleBase:RU004404};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..754
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003695861"
FT DOMAIN 245..322
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 754 AA; 83031 MW; 58FA6A3455164C2D CRC64;
MTFRPALALL FAFIVVAPVC AAQSAADLGA GAKPRKESTL PLKPTADEAQ AAQLSARFLT
RFHYDALPLD DAMSAKIYKA YFKLLDSEKV FFTQQDMAKF AKYKDQLDDA IWNEDLSAPF
DIFNQYVMSA VARMEYARSL LKKGFDFNTN ETYDFDRKHA AWPKDEAALN DLWRKRTMND
WLRLKLAGKS DDEIRKVLDK RYSGYIDRVK QLDGEDAFQT FMTAYAESTD PHTDYLGPRE
AQNFDIAMKL SLEGIGAVLQ ARDDYTQIRE LVPVGPAAKS GKIHVGDRIV GVGQGEKGPI
VDVIGWRLDD VVNLIRGKKD TVVRLEILPA STGLDGKHQL VTLVRKKVTI AEQAAKKKVV
TITDGGVTRK IGVIELPTFY SDFGARREGD KNFKSATRDV AKLLGELKAE GVQGVIVDLR
NNGGGSLYEA NELTGLFIDK GPVVQVRDAR GQVEVQGSDE PKMTWSGPLA VLVNRGTASA
SEIFSAAIQD YGRGLIIGTP TFGKGTVQNL VDLDRFGSAD GKSKPQFGEL KMTIAEFFRI
NGGSTQLKGV TPDIEYPQNG DDKDFGESTY DNALPWTHIA PADYKPVANM KAWLPQLRQM
HDERVAKSPA WKLMLDELAQ YKKMRARTTV SLNFANREAE RKELDAVQTS FRNRHKAIDG
SDAALVDEQS SLDDGLTPGE RSLKQELKEE KDAKKAPDPV LDETAHVLFD AVGLIKAEPK
LAVEVEPYGG KPLADAVAVA PPLQAPPAAT SSAH
//