ID A0A0J5GHT8_9NEIS Unreviewed; 193 AA.
AC A0A0J5GHT8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Peptidase S24 {ECO:0000313|EMBL:KMJ53876.1};
GN ORFNames=ACG97_06485 {ECO:0000313|EMBL:KMJ53876.1};
OS Vogesella sp. EB.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Vogesella.
OX NCBI_TaxID=1526735 {ECO:0000313|EMBL:KMJ53876.1, ECO:0000313|Proteomes:UP000054352};
RN [1] {ECO:0000313|EMBL:KMJ53876.1, ECO:0000313|Proteomes:UP000054352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB {ECO:0000313|EMBL:KMJ53876.1,
RC ECO:0000313|Proteomes:UP000054352};
RA Arrua Day P., Revale S., Alvarez H.M.;
RT "Genome wide analysis of metabolism in the polyhydroxybutyrate-producing
RT Vogesella sp. strain EB.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S24 family.
CC {ECO:0000256|ARBA:ARBA00007484, ECO:0000256|RuleBase:RU003991}.
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:KMJ53876.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFDT01000007; KMJ53876.1; -; Genomic_DNA.
DR RefSeq; WP_047966519.1; NZ_LFDT01000007.1.
DR AlphaFoldDB; A0A0J5GHT8; -.
DR STRING; 1526735.ACG97_06485; -.
DR PATRIC; fig|1526735.3.peg.1389; -.
DR OrthoDB; 9802364at2; -.
DR Proteomes; UP000054352; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR CDD; cd06529; S24_LexA-like; 1.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR InterPro; IPR039418; LexA-like.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR006197; Peptidase_S24_LexA.
DR InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR PANTHER; PTHR33516; LEXA REPRESSOR; 1.
DR PANTHER; PTHR33516:SF13; PROPHAGE REPRESSOR COHE-RELATED; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR PRINTS; PR00726; LEXASERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813,
KW ECO:0000256|RuleBase:RU003991}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003991};
KW Protease {ECO:0000256|ARBA:ARBA00022825};
KW Reference proteome {ECO:0000313|Proteomes:UP000054352};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW SOS mutagenesis {ECO:0000256|ARBA:ARBA00023199};
KW SOS response {ECO:0000256|ARBA:ARBA00023236}.
FT DOMAIN 69..185
FT /note="Peptidase S24/S26A/S26B/S26C"
FT /evidence="ECO:0000259|Pfam:PF00717"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 193 AA; 20997 MW; 3BAE8665A0DC6A3E CRC64;
MSSQGGKREG AGRKSRFGGD KTVAMRVPEP LKPVLENWLD EYRSLRSINH SSIGDIALLG
EALKNLSLPL FASRVPAGSP VAADDLKEAD IDLNQHLVRK PASTFLVTVK GDSMINAGIH
DGDMLVVDRS LEPRNGKVVV AVINDELTVK RLERSAGRVR LLPENPAFKP IEVPEDASFF
IWGVVTNVIH AVD
//
