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Database: UniProt
Entry: U2ZJI2_VIBPR
LinkDB: U2ZJI2_VIBPR
Original site: U2ZJI2_VIBPR 
ID   U2ZJI2_VIBPR            Unreviewed;       355 AA.
AC   U2ZJI2;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=DNA polymerase IV {ECO:0000256|HAMAP-Rule:MF_01113};
DE            Short=Pol IV {ECO:0000256|HAMAP-Rule:MF_01113};
DE            EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_01113};
GN   Name=dinB {ECO:0000256|HAMAP-Rule:MF_01113,
GN   ECO:0000313|EMBL:GAD67901.1};
GN   ORFNames=VPR01S_10_00970 {ECO:0000313|EMBL:GAD67901.1};
OS   Vibrio proteolyticus NBRC 13287.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1219065 {ECO:0000313|EMBL:GAD67901.1, ECO:0000313|Proteomes:UP000016570};
RN   [1] {ECO:0000313|EMBL:GAD67901.1, ECO:0000313|Proteomes:UP000016570}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 13287 {ECO:0000313|EMBL:GAD67901.1,
RC   ECO:0000313|Proteomes:UP000016570};
RA   Isaki S., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y., Tsuchikane K.,
RA   Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A., Fujita N.;
RT   "Whole genome shotgun sequence of Vibrio proteolyticus NBRC 13287.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000256|HAMAP-Rule:MF_01113}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01113};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01113};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01113};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01113}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01113}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-Y family.
CC       {ECO:0000256|ARBA:ARBA00010945, ECO:0000256|HAMAP-Rule:MF_01113}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAD67901.1}.
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DR   EMBL; BATJ01000010; GAD67901.1; -; Genomic_DNA.
DR   AlphaFoldDB; U2ZJI2; -.
DR   STRING; 1219065.VPR01S_10_00970; -.
DR   eggNOG; COG0389; Bacteria.
DR   Proteomes; UP000016570; Unassembled WGS sequence.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProt.
DR   CDD; cd03586; PolY_Pol_IV_kappa; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 3.40.1170.60; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.30.1490.100; DNA polymerase, Y-family, little finger domain; 1.
DR   HAMAP; MF_01113; DNApol_IV; 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; IPR022880; DNApol_IV.
DR   InterPro; IPR024728; PolY_HhH_motif.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001126; UmuC.
DR   PANTHER; PTHR11076:SF33; DNA POLYMERASE KAPPA; 1.
DR   PANTHER; PTHR11076; DNA REPAIR POLYMERASE UMUC / TRANSFERASE FAMILY MEMBER; 1.
DR   Pfam; PF00817; IMS; 1.
DR   Pfam; PF11799; IMS_C; 1.
DR   Pfam; PF11798; IMS_HHH; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF100879; Lesion bypass DNA polymerase (Y-family), little finger domain; 1.
DR   PROSITE; PS50173; UMUC; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01113};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_01113};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01113};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_01113};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01113};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|HAMAP-Rule:MF_01113};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01113};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01113};
KW   Mutator protein {ECO:0000256|ARBA:ARBA00022457, ECO:0000256|HAMAP-
KW   Rule:MF_01113}; Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01113};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016570};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01113}.
FT   DOMAIN          8..189
FT                   /note="UmuC"
FT                   /evidence="ECO:0000259|PROSITE:PS50173"
FT   ACT_SITE        108
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT   BINDING         12
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT   BINDING         107
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT   SITE            17
FT                   /note="Substrate discrimination"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
SQ   SEQUENCE   355 AA;  40765 MW;  E4EC7AFE0433DEC3 CRC64;
     MEKTARKIIH IDMDCFFAAV EMRDNPHYRN RPLAVGGHEK QRGVISTCNY EARRFGVRSA
     MPTARALKLC PQLLVVPGRM EVYKQVSAHI RAIFARYTDK IEPLSLDEAF LDVSECSLCH
     GSATLIAEAI RQDIWTELQL TASAGVAPIK FLAKVASDLN KPNGQTVIPP DQVQQVVDKL
     PLEKIPGVGK VTLEKLHAAG YYLCEDIKQA DYRELLRRFG RLGQSLWKRS HGIDDREVVV
     ARERKSVGVE RTFAENIVSY DQCWQVIEEK LFPELERRLE KVSPEKLISK QGIKLKFADF
     QLTTIEHTHN RLEREYFKVL LRDILKRQQG REIRLLGLSV MLRPELQTKQ LSFFE
//
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