ID A0A380KGI2_9STRE Unreviewed; 781 AA.
AC A0A380KGI2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=ATP-dependent RecD-like DNA helicase {ECO:0000256|HAMAP-Rule:MF_01488};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_01488};
GN Name=recD {ECO:0000313|EMBL:SUN63350.1};
GN Synonyms=recD2 {ECO:0000256|HAMAP-Rule:MF_01488};
GN ORFNames=NCTC12224_02399 {ECO:0000313|EMBL:SUN63350.1};
OS Streptococcus hyointestinalis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1337 {ECO:0000313|EMBL:SUN63350.1, ECO:0000313|Proteomes:UP000254924};
RN [1] {ECO:0000313|EMBL:SUN63350.1, ECO:0000313|Proteomes:UP000254924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12224 {ECO:0000313|EMBL:SUN63350.1,
RC ECO:0000313|Proteomes:UP000254924};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase.
CC Has no activity on blunt DNA or DNA with 3'-overhangs, requires at
CC least 10 bases of 5'-ssDNA for helicase activity. {ECO:0000256|HAMAP-
CC Rule:MF_01488}.
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_01488};
CC -!- SIMILARITY: Belongs to the RecD family. RecD-like subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01488}.
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DR EMBL; UHFN01000007; SUN63350.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A380KGI2; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000254924; Unassembled WGS sequence.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd17933; DEXSc_RecD-like; 1.
DR CDD; cd18809; SF1_C_RecD; 1.
DR Gene3D; 1.10.10.2220; -; 1.
DR Gene3D; 2.30.30.940; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01488; RecD_like; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR006345; DNA_helicase_RecD-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029493; RecD-like_HHH.
DR InterPro; IPR041451; RecD-like_SH13.
DR InterPro; IPR027785; UvrD-like_helicase_C.
DR NCBIfam; TIGR01448; recD_rel; 1.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43788:SF6; RECBCD ENZYME SUBUNIT RECD; 1.
DR Pfam; PF13245; AAA_19; 1.
DR Pfam; PF14490; HHH_4; 1.
DR Pfam; PF18335; SH3_13; 1.
DR Pfam; PF13538; UvrD_C_2; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01488}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_01488};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:SUN63350.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:SUN63350.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}; Reference proteome {ECO:0000313|Proteomes:UP000254924}.
FT DOMAIN 344..499
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 355..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 781 AA; 88453 MW; E8CCA921D0F59394 CRC64;
MEYFFTGSIE RIIFENASNF FKILLLNIED TDSSLDDFEI IVTGIMAEVI EGESYTFWGE
LVEHPKYGEQ LSASRYERKK PSASGLINYF SSSQFKGIGK KTAEKIVTLY GNDPIDAILE
DPSKLDTISG LSKVKKEQFI AQLRLNYGSE QILSKLAEYG ISNRYAMQIF DHYKETTLDV
ITDNPYQLVE DIQGIGFKIA DQLAEQLGIA DDSPKRFRAA LLHCLLNICM NSGDTYVEAR
RLLEETLTLL EQSRQIEIDP ALVANELTQL INDEKIQHVE TKIFDNSLYF SEAGIQKQLH
RILNFELKNL SSDERIEKKL QKVEKELGIS YDSIQRQAIR DALSSKVFIL TGGPGTGKTT
VINGIIQTYA ELHTIDLKKS KDLPIVLAAP TGRASRRMNE LTGLPSATIH RHLGLNRDQE
FQLLDDELDC DLIIIDEFSM VDTWLAHKLF SALPSHAQVI IVGDSDQLPS VGPGQVLADL
LKIPELPKVC LEKIFRQSED STIVTLASQI RQGLLPADFT SKKPDRSYFE AQANYIPDMV
VKIVASALRN GIKAQDVQVL APMYRGQAGI NNLNTLLQEL LNPEKDLSFT FNDMTFRKGD
KVLHLINDAE HNVFNGDIGY ITDLIPAKYT ESKQDELFIN FDGQEVIYAR KDWMRITLAY
AMSIHKSQGS EFPVVILPIT QQSRRMLERN LIYTAITRAK SKLILLGEIS AFDYAIQTQG
TKRHTYLIER FLEQDLPASE KDNDNSNDKE TNQYRLTEEN ITTIDPMIGL SQEEIDFFFK
S
//
