ID H5V0K4_ATLHE Unreviewed; 726 AA.
AC H5V0K4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
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:GAB51512.1};
GN ORFNames=EH105704_03_00160 {ECO:0000313|EMBL:GAB51512.1};
OS Atlantibacter hermannii NBRC 105704.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Atlantibacter.
OX NCBI_TaxID=1115512 {ECO:0000313|EMBL:GAB51512.1, ECO:0000313|Proteomes:UP000010297};
RN [1] {ECO:0000313|EMBL:GAB51512.1, ECO:0000313|Proteomes:UP000010297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105704 {ECO:0000313|EMBL:GAB51512.1,
RC ECO:0000313|Proteomes:UP000010297};
RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Escherichia hermannii NBRC 105704.";
RL Submitted (FEB-2012) 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:GAB51512.1}.
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DR EMBL; BAFF01000003; GAB51512.1; -; Genomic_DNA.
DR RefSeq; WP_002434722.1; NZ_BAFF01000003.1.
DR AlphaFoldDB; H5V0K4; -.
DR eggNOG; COG1199; Bacteria.
DR Proteomes; UP000010297; 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; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR039000; DinG_proteobact.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010614; RAD3-like_helicase_DEAD.
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; PF00270; DEAD; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00488; DEXDc2; 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|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_02205};
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:UP000010297}.
FT DOMAIN 17..294
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT REGION 703..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 120
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02205"
FT BINDING 194
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02205"
FT BINDING 199
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02205"
FT BINDING 205
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02205"
SQ SEQUENCE 726 AA; 82223 MW; 346BA942132192A3 CRC64;
MALSSAQKTQ IAAWYKALQL QIPDFIPRAP QRQMIAEVAK TLAGEEGRHL AIEAPTGVGK
TLSYLIPGIA IARDEQKTLV VSTANVALQD QIFSKDLPLL KKIIPDLRFT AAFGRGRYVC
PRNLSALASS ESTQQDLLAF LDDELTPNSK EEQQFCASLK TDLDGYKWDG LRDHSDKAIE
DDLWRRLSTD KASCLNRNCH YYRECPFFVA RREIQEAEVV VANHALVMAA LESESVLPEP
KNLLLVLDEG HHVPDVARDA LEMSAEITAP WYRLQLDLFS KLIATCLEQF RPKTTPPLAL
PERLNAHCEE LYEHIASLNT LLNLYLPPSQ EAEHRFAMGA LPDEIMEICQ RLAKLTEQLR
GLAELFLNDL SEKTANHDVV RLHRVLLQMN RALGMFESQS KLWRLAAMEK ASGAPVTKWA
TREVREGQLH MFFHCVGIRV SEQLEKLLWR SVPHIVVTSA TLRSLNSFNR LQELSGLKDK
AGDRFVALDS PFNHVEQGKI VIPQMQYEPL IDNEEQHLAE MAAYFRQQVE SKQHLGMLVL
FASGRAMLRF LEYVTDLRLL LLVQGDKPRS RLIQLHRQRV ENGERSVLIG LQSFAEGLDL
KGDLLTQVHI HKIAFPPIDS PVVITEGEWL KSLNRYPFEV QSLPSASFNL IQQVGRLIRS
HECRGEVIIY DKRLLTKNYG KRLLDALPVF PIERPDVPEV TFAKPAASKA RRSKGGAYSR
RKRAGK
//
