ID   UMUC_ECOLI              Reviewed;         422 AA.
AC   P04152;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 165.
DE   RecName: Full=Protein UmuC;
DE   AltName: Full=DNA polymerase V;
DE            Short=Pol V;
GN   Name=umuC; OrderedLocusNames=b1184, JW1173;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2989817; DOI=10.1073/pnas.82.13.4336;
RA   Kitagawa Y., Akaboshi E., Shinagawa H., Horii T., Ogawa H., Kato T.;
RT   "Structural analysis of the umu operon required for inducible mutagenesis
RT   in Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:4336-4340(1985).
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   MUTAGENESIS.
RX   PubMed=1320188; DOI=10.1007/bf00265442;
RA   Koch W.H., Ennis D.G., Levine A.S., Woodgate R.;
RT   "Escherichia coli umuDC mutants: DNA sequence alterations and UmuD
RT   cleavage.";
RL   Mol. Gen. Genet. 233:443-448(1992).
RN   [7]
RP   REGULATION BY LEXA, AND INDUCTION.
RC   STRAIN=K12 / RW118;
RX   PubMed=10760155; DOI=10.1046/j.1365-2958.2000.01826.x;
RA   Fernandez De Henestrosa A.R., Ogi T., Aoyagi S., Chafin D., Hayes J.J.,
RA   Ohmori H., Woodgate R.;
RT   "Identification of additional genes belonging to the LexA regulon in
RT   Escherichia coli.";
RL   Mol. Microbiol. 35:1560-1572(2000).
RN   [8]
RP   FUNCTION IN TRANSLATION REPAIR, AND STIMULATION BY RECA AND BETA
RP   SLIDING-CLAMP COMPLEX.
RX   PubMed=10801133; DOI=10.1038/35010020;
RA   Tang M., Pham P., Shen X., Taylor J.S., O'Donnell M., Woodgate R.,
RA   Goodman M.F.;
RT   "Roles of E. coli DNA polymerases IV and V in lesion-targeted and
RT   untargeted SOS mutagenesis.";
RL   Nature 404:1014-1018(2000).
RN   [9]
RP   INDUCTION BY HYDROXYUREA.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA   Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA   Walker G.C.;
RT   "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT   coli.";
RL   Mol. Cell 36:845-860(2009).
CC   -!- FUNCTION: Involved in UV protection and mutation. Poorly processive,
CC       error-prone DNA polymerase involved in translesion repair
CC       (PubMed:10801133). Essential for induced (or SOS) mutagenesis. Able to
CC       replicate DNA across DNA lesions (thymine photodimers and abasic sites,
CC       translesion synthesis) in the presence of activated RecA; efficiency is
CC       maximal in the presence of the beta sliding-clamp and clamp-loading
CC       complex of DNA polymerase III plus single-stranded binding protein
CC       (SSB) (PubMed:10801133). RecA and to a lesser extent the beta clamp-
CC       complex may target Pol V to replication complexes stalled at DNA
CC       template lesions (PubMed:10801133). {ECO:0000269|PubMed:10801133}.
CC   -!- INTERACTION:
CC       P04152; PRO_0000027305 [P0AG11]: umuD; NbExp=7; IntAct=EBI-1119849, EBI-25426537;
CC   -!- INDUCTION: Repressed by LexA, induced by DNA damage (PubMed:10760155).
CC       Induced 1.5-fold by hydroxyurea (PubMed:20005847).
CC       {ECO:0000269|PubMed:10760155, ECO:0000269|PubMed:20005847}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
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DR   EMBL; M10107; AAA24729.1; -; Genomic_DNA.
DR   EMBL; M13387; AAA98074.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74268.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA36031.1; -; Genomic_DNA.
DR   PIR; E64864; ZWECC.
DR   RefSeq; NP_415702.1; NC_000913.3.
DR   RefSeq; WP_000457616.1; NZ_STEB01000023.1.
DR   AlphaFoldDB; P04152; -.
DR   SMR; P04152; -.
DR   BioGRID; 4261816; 142.
DR   ComplexPortal; CPX-5544; DNA polymerase V mutasome complex.
DR   DIP; DIP-11090N; -.
DR   IntAct; P04152; 11.
DR   STRING; 511145.b1184; -.
DR   PaxDb; P04152; -.
DR   PRIDE; P04152; -.
DR   EnsemblBacteria; AAC74268; AAC74268; b1184.
DR   EnsemblBacteria; BAA36031; BAA36031; BAA36031.
DR   GeneID; 66674996; -.
DR   GeneID; 946359; -.
DR   KEGG; ecj:JW1173; -.
DR   KEGG; eco:b1184; -.
DR   PATRIC; fig|1411691.4.peg.1103; -.
DR   EchoBASE; EB1049; -.
DR   eggNOG; COG0389; Bacteria.
DR   HOGENOM; CLU_012348_3_0_6; -.
DR   InParanoid; P04152; -.
DR   OMA; YRYEPHR; -.
DR   PhylomeDB; P04152; -.
DR   BioCyc; EcoCyc:EG11056-MON; -.
DR   BioCyc; MetaCyc:EG11056-MON; -.
DR   PRO; PR:P04152; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009355; C:DNA polymerase V complex; IDA:EcoCyc.
DR   GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
DR   GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:EcoCyc.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:EcoCyc.
DR   GO; GO:0003697; F:single-stranded DNA binding; IDA:EcoCyc.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR   GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR   GO; GO:0009432; P:SOS response; IDA:ComplexPortal.
DR   GO; GO:0019985; P:translesion synthesis; IDA:EcoCyc.
DR   Gene3D; 3.30.1490.100; -; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR   InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR   InterPro; IPR025188; DUF4113.
DR   InterPro; IPR024728; PolY_HhH_motif.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001126; UmuC.
DR   Pfam; PF13438; DUF4113; 1.
DR   Pfam; PF00817; IMS; 1.
DR   Pfam; PF11799; IMS_C; 1.
DR   Pfam; PF11798; IMS_HHH; 1.
DR   SUPFAM; SSF100879; SSF100879; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS50173; UMUC; 1.
PE   1: Evidence at protein level;
KW   DNA damage; DNA repair; Reference proteome; SOS mutagenesis; SOS response.
FT   CHAIN           1..422
FT                   /note="Protein UmuC"
FT                   /id="PRO_0000173982"
FT   DOMAIN          2..188
FT                   /note="UmuC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   MUTAGEN         75
FT                   /note="E->K: In umuC36; non-mutable."
FT                   /evidence="ECO:0000269|PubMed:1320188"
FT   MUTAGEN         101
FT                   /note="D->N: In umuC104; non-mutable."
FT                   /evidence="ECO:0000269|PubMed:1320188"
FT   MUTAGEN         290
FT                   /note="T->K: In umuC25; non-mutable."
FT                   /evidence="ECO:0000269|PubMed:1320188"
FT   CONFLICT        152
FT                   /note="A -> E (in Ref. 1; AAA24729)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   422 AA;  47680 MW;  0F1855D802A3F5F8 CRC64;
     MFALCDVNAF YASCETVFRP DLWGKPVVVL SNNDGCVIAR NAEAKALGVK MGDPWFKQKD
     LFRRCGVVCF SSNYELYADM SNRVMSTLEE LSPRVEIYSI DEAFCDLTGV RNCRDLTDFG
     REIRATVLQR THLTVGVGIA QTKTLAKLAN HAAKKWQRQT GGVVDLSNLE RQRKLMSALP
     VDDVWGIGRR ISKKLDAMGI KTVLDLADTD IRFIRKHFNV VLERTVRELR GEPCLQLEEF
     APTKQEIICS RSFGERITDY PSMRQAICSY AARAAEKLRS EHQYCRFIST FIKTSPFALN
     EPYYGNSASV KLLTPTQDSR DIINAATRSL DAIWQAGHRY QKAGVMLGDF FSQGVAQLNL
     FDDNAPRPGS EQLMTVMDTL NAKEGRGTLY FAGQGIQQQW QMKRAMLSPR YTTRSSDLLR
     VK