ID   MUCA_ECOLX              Reviewed;         146 AA.
AC   P0A276; P07376; P14302;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Protein MucA;
DE            EC=3.4.21.-;
DE   Contains:
DE     RecName: Full=Protein MucA';
GN   Name=mucA;
OS   Escherichia coli.
OG   Plasmid IncN pKM101.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Tanooka H.;
RL   Submitted (MAY-1990) to the PIR data bank.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2989816; DOI=10.1073/pnas.82.13.4331;
RA   Perry K.L., Elledge S.J., Mitchell B.B., Marsh L., Walker G.C.;
RT   "umuDC and mucAB operons whose products are required for UV light- and
RT   chemical-induced mutagenesis: UmuD, MucA, and LexA proteins share
RT   homology.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:4331-4335(1985).
CC   -!- FUNCTION: Involved in UV protection and mutation.
CC   -!- MISCELLANEOUS: The mucAB operon is the plasmid-borne analog of the
CC       E.coli umuDC operon.
CC   -!- SIMILARITY: Belongs to the peptidase S24 family. {ECO:0000305}.
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DR   EMBL; D90147; BAA14175.1; -; Genomic_DNA.
DR   EMBL; M13388; AAA98277.1; -; Genomic_DNA.
DR   PIR; D23157; ZWECAP.
DR   RefSeq; WP_000861760.1; NZ_WWEL01000030.1.
DR   RefSeq; YP_001096389.1; NC_009132.1.
DR   RefSeq; YP_004558175.1; NC_015599.1.
DR   RefSeq; YP_006903037.1; NC_019033.1.
DR   RefSeq; YP_006953654.1; NC_019082.1.
DR   RefSeq; YP_006954516.1; NC_019098.1.
DR   RefSeq; YP_008574883.1; NC_022374.1.
DR   RefSeq; YP_008826439.1; NC_022885.1.
DR   RefSeq; YP_009023174.1; NC_023909.1.
DR   RefSeq; YP_009023255.1; NC_023910.1.
DR   RefSeq; YP_009060618.1; NC_024967.1.
DR   RefSeq; YP_009061018.1; NC_024974.1.
DR   RefSeq; YP_009068558.1; NC_025141.1.
DR   RefSeq; YP_009071547.1; NC_025183.1.
DR   RefSeq; YP_724516.1; NC_007682.3.
DR   AlphaFoldDB; P0A276; -.
DR   SMR; P0A276; -.
DR   MEROPS; S24.003; -.
DR   GeneID; 64209521; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR   CDD; cd06529; S24_LexA-like; 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   Pfam; PF00717; Peptidase_S24; 1.
DR   PRINTS; PR00726; LEXASERPTASE.
DR   SUPFAM; SSF51306; SSF51306; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; DNA damage; DNA repair; Hydrolase; Plasmid;
KW   Protease; Serine protease; SOS mutagenesis; SOS response.
FT   CHAIN           1..146
FT                   /note="Protein MucA"
FT                   /id="PRO_0000041985"
FT   CHAIN           27..146
FT                   /note="Protein MucA'"
FT                   /id="PRO_0000027299"
FT   ACT_SITE        62
FT                   /note="For autocatalytic cleavage activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        99
FT                   /note="For autocatalytic cleavage activity"
FT                   /evidence="ECO:0000250"
FT   SITE            26..27
FT                   /note="Cleavage; by autolysis"
FT   CONFLICT        13
FT                   /note="Missing (in Ref. 2; AAA98277)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   146 AA;  16527 MW;  7605A681F8345E76 CRC64;
     MKVDIFESSG ASRVHSIPFY LQRISAGFPS PAQGYEKQEL NLHEYCVRHP SATYFLRVSG
     SSMEDGRIHD GDVLVVDRSL TASHGSIVVA CIHNEFTVKR LLLRPRPCLM PMNKDFPVYY
     IDPDNESVEI WGVVTHSLIE HPVCLR