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Database: UniProt
Entry: F0EWR8_9NEIS
LinkDB: F0EWR8_9NEIS
Original site: F0EWR8_9NEIS 
ID   F0EWR8_9NEIS            Unreviewed;       727 AA.
AC   F0EWR8;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=ATP-dependent DNA helicase DinG {ECO:0000256|HAMAP-Rule:MF_02205};
DE            EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_02205};
GN   Name=dinG {ECO:0000256|HAMAP-Rule:MF_02205,
GN   ECO:0000313|EMBL:EGC18149.1};
GN   ORFNames=HMPREF9098_0298 {ECO:0000313|EMBL:EGC18149.1};
OS   Kingella denitrificans ATCC 33394.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Kingella.
OX   NCBI_TaxID=888741 {ECO:0000313|EMBL:EGC18149.1, ECO:0000313|Proteomes:UP000004088};
RN   [1] {ECO:0000313|EMBL:EGC18149.1, ECO:0000313|Proteomes:UP000004088}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33394 {ECO:0000313|EMBL:EGC18149.1,
RC   ECO:0000313|Proteomes:UP000004088};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase.
CC       {ECO:0000256|HAMAP-Rule:MF_02205}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02205};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02205};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_02205};
CC   -!- SIMILARITY: Belongs to the helicase family. DinG subfamily. Type 1 sub-
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_02205}.
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:EGC18149.1}.
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DR   EMBL; AEWV01000006; EGC18149.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0EWR8; -.
DR   STRING; 888741.HMPREF9098_0298; -.
DR   HOGENOM; CLU_012117_4_1_4; -.
DR   Proteomes; UP000004088; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_02205; DinG_proteobact; 1.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR045028; DinG/Rad3-like.
DR   InterPro; IPR039000; DinG_proteobact.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11472:SF59; ATP-DEPENDENT DNA HELICASE DING; 1.
DR   PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   SMART; SM00491; HELICc2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_02205};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_02205}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_02205};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_02205, ECO:0000313|EMBL:EGC18149.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_02205};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_02205};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02205};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02205};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02205}; Reference proteome {ECO:0000313|Proteomes:UP000004088}.
FT   DOMAIN          31..335
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
FT   BINDING         148
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02205"
FT   BINDING         224
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02205"
FT   BINDING         229
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02205"
FT   BINDING         235
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02205"
SQ   SEQUENCE   727 AA;  81158 MW;  525D9A25D549C711 CRC64;
     MQIQTSPKAA CTPSAMLTEL EKNAIRDHYR ALSENLPNFR PRTAQREMIA AIANAFSRTK
     TQKEGEEAPK REGESIVVIE GPTGVGKSLA YLLAGGIMAQ TRGKRLIVSS ATVALQEQLV
     GRDLPFVVEK SGLELSFAIA KGRGRYLCPY KLYQLTQTHA QQSLTGFEQP ALLWDSKPKK
     EELDTLHQMA DRFSRRQFDG DRDTWQEKID DSLWKKVAND PHSCLKSACP NRPECPFFLA
     RDTLDTVDVV VCNHDLLMVD IGMGGGVILP PPEHSFYCID EAHHLSKKAL NQLAAEHSWL
     QAMWTLEKLP AQTAKIAMLC DKAELANLAD EAAAALLDCM NEWQFHLQDE PSFQEADSTH
     ESVWLWDNGE IPEELTALVH NCHISAQSLL KHLYSLRDAL SAARRDKDQN SVQIDRTAAD
     FGLFVGRGEE IADLWQLMST TRQSEQEEPL AKWISRRLTD NKTDWQFHAS PISSAQQLAN
     RFWRRAAGVV LTSATLQSLG NFNLLLRQTG LNWLPETSTL ALQSPFDFTA QGELYLPPMS
     ASPKDSAAHT AEIAEWLPRL ISDSEPIGTL VLFSSRKQMQ EVALRLPAAY LPLLLIQGEQ
     SKSRLLQQHH DAIAAGRPSI IFGLDSFAEG LDLPGNACVH VIIAKLPFSM PDNPIEKTQS
     NWIKQRGGNP FMEITVPEAA IKLVQAVGRL IRTEQDYGRI TILDNRIQTQ RYGQQLLAGL
     PPFKRIG
//
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