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Database: UniProt
Entry: Q8GFX8_CITFR
LinkDB: Q8GFX8_CITFR
Original site: Q8GFX8_CITFR 
ID   Q8GFX8_CITFR            Unreviewed;       144 AA.
AC   Q8GFX8;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   SubName: Full=MucA {ECO:0000313|EMBL:AAN87630.1};
GN   Name=mucA {ECO:0000313|EMBL:AAN87630.1};
OS   Citrobacter freundii.
OG   Plasmid pCTX-M3 {ECO:0000313|EMBL:AAN87630.1}.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX   NCBI_TaxID=546 {ECO:0000313|EMBL:AAN87630.1};
RN   [1] {ECO:0000313|EMBL:AAN87630.1}
RP   NUCLEOTIDE SEQUENCE.
RC   PLASMID=pCTX-M3 {ECO:0000313|EMBL:AAN87630.1};
RX   PubMed=17698626; DOI=10.1128/AAC.00457-07;
RA   Golebiewski M., Kern-Zdanowicz I., Zienkiewicz M., Adamczyk M.,
RA   Zylinska J., Baraniak A., Gniadkowski M., Bardowski J., Ceglowski P.;
RT   "Complete nucleotide sequence of the pCTX-M3 plasmid and its involvement in
RT   spread of the extended-spectrum beta-lactamase gene blaCTX-M-3.";
RL   Antimicrob. Agents Chemother. 51:3789-3795(2007).
CC   -!- SIMILARITY: Belongs to the peptidase S24 family.
CC       {ECO:0000256|ARBA:ARBA00007484, ECO:0000256|RuleBase:RU003991}.
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DR   EMBL; AF550415; AAN87630.1; -; Genomic_DNA.
DR   RefSeq; NP_774966.1; NC_004464.2.
DR   RefSeq; WP_011091030.1; NZ_MH722216.1.
DR   AlphaFoldDB; Q8GFX8; -.
DR   MEROPS; S24.003; -.
DR   GeneID; 83649047; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
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   Plasmid {ECO:0000313|EMBL:AAN87630.1};
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          20..132
FT                   /note="Peptidase S24/S26A/S26B/S26C"
FT                   /evidence="ECO:0000259|Pfam:PF00717"
SQ   SEQUENCE   144 AA;  15964 MW;  359782829F727F67 CRC64;
     MALDLVYPRP SVEGAALPFF AEPVAAGFPS PAAGYEANEL NLHDYCVRRP AATYFLRVSG
     DSMRDARIHD GDVLVVDRAE EPRHGSIVIA SIDNEFTVKQ LQLRPYPCLM PLNPAFPPIR
     FDPEALQIWG VVTFTVMSHR PCTP
//
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