ID A0A174R971_9BACE Unreviewed; 363 AA.
AC A0A174R971;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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:CUP79570.1};
GN ORFNames=DW190_02705 {ECO:0000313|EMBL:RHH95162.1}, DWY26_14595
GN {ECO:0000313|EMBL:RGR69101.1}, DXA49_17100
GN {ECO:0000313|EMBL:RGY23464.1}, ERS852494_03108
GN {ECO:0000313|EMBL:CUP79570.1}, ERS852558_03703
GN {ECO:0000313|EMBL:CUQ48314.1}, F2Y31_20465
GN {ECO:0000313|EMBL:KAA5494820.1}, F2Y35_10700
GN {ECO:0000313|EMBL:KAA5491833.1}, F2Y39_13235
GN {ECO:0000313|EMBL:KAA5475861.1}, NXW23_08910
GN {ECO:0000313|EMBL:UVQ98409.1};
OS Bacteroides caccae.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=47678 {ECO:0000313|EMBL:CUP79570.1, ECO:0000313|Proteomes:UP000095657};
RN [1] {ECO:0000313|Proteomes:UP000095657, ECO:0000313|Proteomes:UP000095725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5834880 {ECO:0000313|EMBL:CUP79570.1,
RC ECO:0000313|Proteomes:UP000095657}, and 2789STDY5834946
RC {ECO:0000313|EMBL:CUQ48314.1, ECO:0000313|Proteomes:UP000095725};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000283512, ECO:0000313|Proteomes:UP000284205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF24-29LB {ECO:0000313|EMBL:RGR69101.1,
RC ECO:0000313|Proteomes:UP000284205}, AM16-49B
RC {ECO:0000313|EMBL:RHH95162.1, ECO:0000313|Proteomes:UP000283512}, and
RC OF02-6LB {ECO:0000313|EMBL:RGY23464.1,
RC ECO:0000313|Proteomes:UP000284431};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000368418, ECO:0000313|Proteomes:UP000427825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIOML-A19 {ECO:0000313|EMBL:KAA5494820.1,
RC ECO:0000313|Proteomes:UP000368418}, BIOML-A21
RC {ECO:0000313|EMBL:KAA5491833.1, ECO:0000313|Proteomes:UP000491168},
RC and BIOML-A25 {ECO:0000313|EMBL:KAA5475861.1,
RC ECO:0000313|Proteomes:UP000427825};
RX PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA Xavier R.J., Alm E.J.;
RT "A library of human gut bacterial isolates paired with longitudinal
RT multiomics data enables mechanistic microbiome research.";
RL Nat. Med. 25:1442-1452(2019).
RN [4] {ECO:0000313|EMBL:UVQ98409.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BFG-474 {ECO:0000313|EMBL:UVQ98409.1};
RA Tisza M.J., Smith D., Dekker J.P.;
RT "Genome Sequencing of Bacteroides fragilis Group Isolates with Nanopore
RT Technology.";
RL Submitted (AUG-2022) 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}.
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DR EMBL; CZAI01000007; CUP79570.1; -; Genomic_DNA.
DR EMBL; CZBL01000018; CUQ48314.1; -; Genomic_DNA.
DR EMBL; VVYJ01000007; KAA5475861.1; -; Genomic_DNA.
DR EMBL; VVYF01000009; KAA5491833.1; -; Genomic_DNA.
DR EMBL; VVYD01000028; KAA5494820.1; -; Genomic_DNA.
DR EMBL; QRUO01000014; RGR69101.1; -; Genomic_DNA.
DR EMBL; QSCS01000030; RGY23464.1; -; Genomic_DNA.
DR EMBL; QRKD01000001; RHH95162.1; -; Genomic_DNA.
DR EMBL; CP103166; UVQ98409.1; -; Genomic_DNA.
DR RefSeq; WP_022042486.1; NZ_WQQZ01000048.1.
DR STRING; 47678.ERS852494_03108; -.
DR Proteomes; UP000095657; Unassembled WGS sequence.
DR Proteomes; UP000095725; Unassembled WGS sequence.
DR Proteomes; UP000283512; Unassembled WGS sequence.
DR Proteomes; UP000284205; Unassembled WGS sequence.
DR Proteomes; UP000284431; Unassembled WGS sequence.
DR Proteomes; UP000368418; Unassembled WGS sequence.
DR Proteomes; UP000427825; Unassembled WGS sequence.
DR Proteomes; UP000491168; Unassembled WGS sequence.
DR Proteomes; UP001060260; 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; 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|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|HAMAP-Rule:MF_01113};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01113,
KW ECO:0000313|EMBL:CUP79570.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095657};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01113, ECO:0000313|EMBL:CUP79570.1}.
FT DOMAIN 6..186
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT ACT_SITE 105
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT BINDING 104
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT SITE 15
FT /note="Substrate discrimination"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
SQ SEQUENCE 363 AA; 41474 MW; 464985CB47FAFB9C CRC64;
MVQRKIIHID MDAFYASVEQ RDHPELRGKP LAVGHAEERG VVAAASYEAR RYGVRSAMSS
QKAKRLCPQL IFVPGRMDVY KSVSRQIHEI FHEYTDIIEP LSLDEAFLDV TENKKGISLA
VDIAKEIKQK IRDQLNLVAS AGISYNKFLA KIASDYRKPD GLCTIHPEQA LEFIARLPIE
SFWGVGPVTA KRMHLLGIRN GLQLRKCSLE TLTAHFGKVG SLYYECARGI DERPVEAVRI
RKSIGCERTL ERDISSRSSV IIELYHMAVE LIERLQRKEF KGNTLTLKIK FHDFSQITRS
ITQSQELTTL DRVLPLAKEL LKTVEYEQHP IRLIGLSVSN PKEEADEQHG VWEQLSFEFS
DWE
//
