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Protein data for DPO4_SALTI:

Description:
DNA polymerase IV (EC 2.7.7.7) (Pol IV).

Molecular weight: 39658

View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):

DNA repair( GO:0006281 )


Important dates:
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
07-MAR-2006, entry version 12.

Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Enterobacteriales Enterobacteriaceae Salmonella.

To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html

Links to references in other databases for protein DPO4_SALTI:

DatabasePointerAdd. info#1Add. info#2
EMBLAL627266CAD08783.1-
EMBLAE014613AAO70121.1-
HSSPP960221IM4
SMRP63990243-351.1
GenomeReviewsAL513382_GRSTY0358.1
GenomeReviewsAE014613_GRt2537.1
HAMAPMF_01113-1.
InterProIPR001126UMUC_like.
PfamPF00817IMS1.
PROSITEPS50173UMUC1.

General information about the databases mentioned above

Keywords:
Complete proteome; DNA damage; DNA repair; DNA replication; DNA-binding; DNA-directed DNA polymerase; Magnesium; Metal-binding; Mutator protein; Nucleotidyltransferase; Transferase.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX MEDLINE=21534947; PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P.,
RA Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J.,
RA Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K.,
RA Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C.,
RA Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K.,
RA Whitehead S., Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella
RT enterica serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ty2 / ATCC 700931;
RX MEDLINE=22531367; PubMed=12644504;
RX DOI=10.1128/JB.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J.,
RA Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2
RT and CT18.";
RL J. Bacteriol. 185:2330-2337(2003).

Feature:
CHAIN 1 351 DNA polymerase IV.
/FTId=PRO_0000173942.
DOMAIN 4 185 UmuC.
ACT_SITE 104 104 By similarity.
METAL 8 8 Magnesium (By similarity).
METAL 103 103 Magnesium (By similarity).
SITE 13 13 Substrate discrimination (By similarity).

Comments:
-!- FUNCTION: Poorly processive, error-prone DNA polymerase involved
in untargeted mutagenesis. Copies undamaged DNA at stalled
replication forks, which arise in vivo from mismatched or
misaligned primer ends. These misaligned primers can be extended
by polIV. Exhibits no 3'-5' exonuclease (proofreading) activity.
May be involved in translesional synthesis, in conjunction with
the beta clamp from polIII (By similarity).
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
-!- SUBUNIT: Monomer (By similarity).
-!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
-!- SIMILARITY: Belongs to the DNA polymerase type-Y family.
-!- SIMILARITY: Contains 1 umuC domain.
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Sequence length: 351

     MRKIIHVDMD CFFAAVEMRD NPALRDIPIA IGGSRERRGV ISTANYPARQ FGVRSAMPTA
     MALKLCPHLT LLPGRFDAYK EASRHVRDIF SRYTSLIEPL SLDEAWLDVT DSPHCYGSAT
     LIAREIRQTI FNELQLTASA GVAPVKFLAK IASDLNKPNG QYVITPADVP DFLKTLPLAK
     IPGVGKVSAA KLENMGLRTC GDIQQCDLAM LLKRFGKFGR VLWERSQGID ERDVNSERLR
     KSVGVERTLA EDIHEWSDCE AIIEHLYPEL ERRLAIVKPD LLIARQGVKL KFNDFQQTTQ
     EHVWPQLNKE DLITTARKTW DERRGERGVR LVGLHVTLLD PQLERQLVLG L

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