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Database: UniProt
Entry: A0A1H0N2K7_9GAMM
LinkDB: A0A1H0N2K7_9GAMM
Original site: A0A1H0N2K7_9GAMM 
ID   A0A1H0N2K7_9GAMM        Unreviewed;       146 AA.
AC   A0A1H0N2K7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=SOS response UmuD protein. Serine peptidase. MEROPS family S24 {ECO:0000313|EMBL:SDO86887.1};
GN   ORFNames=SAMN04487957_1148 {ECO:0000313|EMBL:SDO86887.1};
OS   Halomonas shengliensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=419597 {ECO:0000313|EMBL:SDO86887.1, ECO:0000313|Proteomes:UP000199075};
RN   [1] {ECO:0000313|Proteomes:UP000199075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6444 {ECO:0000313|Proteomes:UP000199075};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S24 family.
CC       {ECO:0000256|ARBA:ARBA00007484, ECO:0000256|RuleBase:RU003991}.
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DR   EMBL; FNIV01000014; SDO86887.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0N2K7; -.
DR   STRING; 419597.SAMN04487957_1148; -.
DR   OrthoDB; 9787787at2; -.
DR   Proteomes; UP000199075; 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   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   SOS mutagenesis {ECO:0000256|ARBA:ARBA00023199};
KW   SOS response {ECO:0000256|ARBA:ARBA00023236}.
FT   DOMAIN          31..137
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"
FT   COMPBIAS        1..20
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   146 AA;  16092 MW;  876B6CE5ACD3F7E6 CRC64;
     MPHAKFTPAD PAPPPMALPH PLARTRAGIS GFPSPAQDYE GRTLDLNERL VKRPSASFFM
     TVTGDSMDSL GIHDGDLLLI DRSIEPRPGH ILVALVEGEI TVKRYQLKGR QPYLCSANPA
     YPPIPLEDLD CQIWGVVRSV IHEYPV
//
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