ID R4WG74_KLEPN Unreviewed; 141 AA.
AC R4WG74;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=DNA polymerase V subunit D {ECO:0000313|EMBL:BAN19300.1};
GN Name=umuD {ECO:0000313|EMBL:BAN19300.1};
GN ORFNames=KPX_A0075 {ECO:0000313|EMBL:BAN19300.1};
OS Klebsiella pneumoniae subsp. pneumoniae KPX.
OG Plasmid pKPX-1 {ECO:0000313|EMBL:BAN19300.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=990925 {ECO:0000313|EMBL:BAN19300.1};
RN [1] {ECO:0000313|EMBL:BAN19300.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KPX {ECO:0000313|EMBL:BAN19300.1};
RC PLASMID=pKPX-1 {ECO:0000313|EMBL:BAN19300.1};
RX PubMed=23658651; DOI=10.1371/journal.pone.0062774;
RA Huang T.W., Chen T.L., Chen Y.T., Lauderdale T.L., Liao T.L., Lee Y.T.,
RA Chen C.P., Liu Y.M., Lin A.C., Chang Y.H., Wu K.M., Kirby R., Lai J.F.,
RA Tan M.C., Siu L.K., Chang C.M., Fung C.P., Tsai S.F.;
RT "Copy Number Change of the NDM-1 Sequence in a Multidrug-Resistant
RT Klebsiella pneumoniae Clinical Isolate.";
RL PLoS ONE 8:e62774-e62774(2013).
CC -!- SIMILARITY: Belongs to the peptidase S24 family.
CC {ECO:0000256|ARBA:ARBA00007484, ECO:0000256|RuleBase:RU003991}.
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DR EMBL; AP012055; BAN19300.1; -; Genomic_DNA.
DR RefSeq; WP_004178083.1; NC_021198.1.
DR RefSeq; YP_007969487.1; NC_021198.1.
DR AlphaFoldDB; R4WG74; -.
DR MEROPS; S24.003; -.
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 Plasmid {ECO:0000313|EMBL:BAN19300.1};
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 16..130
FT /note="Peptidase S24/S26A/S26B/S26C"
FT /evidence="ECO:0000259|Pfam:PF00717"
SQ SEQUENCE 141 AA; 15795 MW; 0B71BCF0DD586797 CRC64;
MKFIPAVSEA SIVKIPLFTE RCPAGFPSPA SDYTESELDL NEYCIHRRHS TYFVRAIGNS
MTDIGLYSGD LLVVDKAEQP RHGDIVIAEI EGEFTVKRLL LTPRPALQAM NPDFPSLYPD
PETLQIFGVV TAFIHKTRRA D
//
