(data stored in SCRATCH zone)

SWISSPROT: DPO41_BACSU

ID   DPO41_BACSU             Reviewed;         414 AA.
AC   P54545;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   11-DEC-2019, entry version 133.
DE   RecName: Full=DNA polymerase IV 1;
DE            Short=Pol IV 1;
DE            EC=2.7.7.7;
GN   Name=dinB1; Synonyms=yqjH; OrderedLocusNames=BSU23870;
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).
RN   [3]
RP   SEQUENCE REVISION TO 331.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
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; BAA12614.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14319.2; -; Genomic_DNA.
DR   PIR; H69963; H69963.
DR   RefSeq; NP_390268.2; NC_000964.3.
DR   RefSeq; WP_004398755.1; NZ_JNCM01000036.1.
DR   SMR; P54545; -.
DR   IntAct; P54545; 2.
DR   STRING; 224308.BSU23870; -.
DR   PaxDb; P54545; -.
DR   PRIDE; P54545; -.
DR   EnsemblBacteria; CAB14319; CAB14319; BSU23870.
DR   GeneID; 938691; -.
DR   KEGG; bsu:BSU23870; -.
DR   PATRIC; fig|224308.179.peg.2600; -.
DR   eggNOG; ENOG4105CQ3; Bacteria.
DR   eggNOG; COG0389; LUCA.
DR   HOGENOM; HOG000082710; -.
DR   InParanoid; P54545; -.
DR   KO; K02346; -.
DR   OMA; KVRRYDF; -.
DR   PhylomeDB; P54545; -.
DR   BioCyc; BSUB:BSU23870-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   CDD; cd03586; PolY_Pol_IV_kappa; 1.
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; IPR024728; PolY_HhH_motif.
DR   InterPro; IPR001126; UmuC.
DR   Pfam; PF00817; IMS; 1.
DR   Pfam; PF11799; IMS_C; 1.
DR   Pfam; PF11798; IMS_HHH; 1.
DR   SUPFAM; SSF100879; SSF100879; 1.
DR   PROSITE; PS50173; UMUC; 1.
PE   3: Inferred from homology;
DR   PRODOM; P54545.
DR   SWISS-2DPAGE; P54545.
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..414
FT                   /note="DNA polymerase IV 1"
FT                   /id="PRO_0000173904"
FT   DOMAIN          8..189
FT                   /note="UmuC"
FT   ACT_SITE        109
FT                   /evidence="ECO:0000250"
FT   METAL           12
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   METAL           108
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   SITE            17
FT                   /note="Substrate discrimination"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        331
FT                   /note="N -> K (in Ref. 1; BAA12614)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   414 AA;  47006 MW;  0D71C62630BEF23F CRC64;
     MPGKSRIIFH IDMNSFYASV EMAYDPALRG KPVAVAGNVK ERKGIVVTCS YEARARGVKT
     TMPVWQAKRH CPELIVLPPN FDRYRNSSRA MFTILREYTD LVEPVSIDEG YMDMTDTPYS
     SRALETAKEI QSRLQKELLL PSSIGIAPNK FLAKMASDMK KPLGITILRK RQVPDILWPL
     PVGEMHGVGK KTAEKLKGLG IHTIGELAAA DEHSLKRLLG INGPRLKNKA NGIHHAPVDP
     ERIYEFKSVG NSSTLSHDSS DEEELLGVFR KLAASVSDRL QRKEVMASKL FIMIRYADWR
     TITRSTTLRN PIDQKNDILK EAEHLFFKHW NKNPVRLLGI TGTDLVEKEQ AYKQLDLFSF
     NEDAKDEPIQ QMMEKLNKKY GTKLIRKGAT LKKEESKTKG TSFNKDFFQD EKKS
//

If you have problems or comments...

PBIL Back to PBIL home page