(data stored in SCRATCH zone)

SWISSPROT: DPO42_BACSU

ID   DPO42_BACSU             Reviewed;         412 AA.
AC   P54560;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   11-DEC-2019, entry version 124.
DE   RecName: Full=DNA polymerase IV 2;
DE            Short=Pol IV 2;
DE            EC=2.7.7.7;
GN   Name=dinB2; Synonyms=yqjW; OrderedLocusNames=BSU23710;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- FUNCTION: Poorly processive, error-prone DNA polymerase involved in
CC       untargeted mutagenesis. Copies undamaged DNA at stalled replication
CC       forks, which arise in vivo from mismatched or misaligned primer ends.
CC       These misaligned primers can be extended by PolIV. Exhibits no 3'-5'
CC       exonuclease (proofreading) activity. May be involved in translesional
CC       synthesis, in conjunction with the beta clamp from PolIII (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:11130,
CC         Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:83828; EC=2.7.7.7;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
DR   EMBL; D84432; BAA12629.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14303.1; -; Genomic_DNA.
DR   PIR; G69965; G69965.
DR   RefSeq; NP_390252.1; NC_000964.3.
DR   RefSeq; WP_010886562.1; NZ_JNCM01000036.1.
DR   SMR; P54560; -.
DR   IntAct; P54560; 1.
DR   STRING; 224308.BSU23710; -.
DR   PaxDb; P54560; -.
DR   PRIDE; P54560; -.
DR   EnsemblBacteria; CAB14303; CAB14303; BSU23710.
DR   GeneID; 938705; -.
DR   KEGG; bsu:BSU23710; -.
DR   PATRIC; fig|224308.43.peg.2473; -.
DR   eggNOG; ENOG4105CQ3; Bacteria.
DR   eggNOG; COG0389; LUCA.
DR   HOGENOM; HOG000082710; -.
DR   InParanoid; P54560; -.
DR   KO; K02346; -.
DR   OMA; DMQSFYA; -.
DR   PhylomeDB; P54560; -.
DR   BioCyc; BSUB:BSU23710-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR   GO; GO:0009432; P:SOS response; IBA:GO_Central.
DR   GO; GO:0019985; P:translesion synthesis; IBA:GO_Central.
DR   Gene3D; 3.30.1490.100; -; 1.
DR   HAMAP; MF_01113; DNApol_IV; 1.
DR   InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR   InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR   InterPro; IPR022880; DNApol_IV.
DR   InterPro; IPR001126; UmuC.
DR   Pfam; PF00817; IMS; 1.
DR   Pfam; PF11799; IMS_C; 1.
DR   SUPFAM; SSF100879; SSF100879; 1.
DR   PROSITE; PS50173; UMUC; 1.
PE   3: Inferred from homology;
DR   PRODOM; P54560.
DR   SWISS-2DPAGE; P54560.
KW   Cytoplasm; DNA damage; DNA repair; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Magnesium; Metal-binding; Mutator protein;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..412
FT                   /note="DNA polymerase IV 2"
FT                   /id="PRO_0000173905"
FT   DOMAIN          7..192
FT                   /note="UmuC"
FT   ACT_SITE        108
FT                   /evidence="ECO:0000250"
FT   METAL           11
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   METAL           107
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   SITE            16
FT                   /note="Substrate discrimination"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   412 AA;  45944 MW;  5D72B0F505FB96DC CRC64;
     MMKEKVIFLV DMQSFYASVE KAENPHLKNR PVIVSGDPEK RGGVVLAACP LAKQKGVVNA
     SRLWEAQEKC PEAVVLRPRM QRYIDVSLQI TAILEEYTDL VEPYSIDEQF MDITGSQKLF
     GTPMEIAKSI QGRIMREIGV YARVGIGPNK ALAKIACDNF AKKNKNGIFT LTKENMKTEM
     WPLPVGSMFG VGSRMKHHLN RMGISTIGGL AAFPLDLLKK KWGINGHVLW MTANGIDYSP
     VSTSSLDGQK AIGHGMTLPR DYEHFDKEIK VVLLELSEEV CRRSRNAGVM GQTVSVSCRG
     ADFDWPTGFN RQVKLAEPTN STQDVYEAVR RLFLTFWDGK PVRRLGVNLS QLSSDDIWQL
     NLFQDYAKKM SLGYVMDGIK NRFGDTAIIR AASLTAAGQA FERAAKIGGH YK
//

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