ID Q1JF61_STRPD Unreviewed; 817 AA.
AC Q1JF61;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
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:ABF34698.1};
GN Synonyms=recD2 {ECO:0000256|HAMAP-Rule:MF_01488};
GN OrderedLocusNames=MGAS10270_Spy1633 {ECO:0000313|EMBL:ABF34698.1};
OS Streptococcus pyogenes serotype M2 (strain MGAS10270).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370552 {ECO:0000313|EMBL:ABF34698.1, ECO:0000313|Proteomes:UP000002436};
RN [1] {ECO:0000313|EMBL:ABF34698.1, ECO:0000313|Proteomes:UP000002436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS10270 {ECO:0000313|EMBL:ABF34698.1,
RC ECO:0000313|Proteomes:UP000002436};
RX PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA Musser J.M.;
RT "Molecular genetic anatomy of inter- and intraserotype variation in the
RT human bacterial pathogen group A Streptococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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; CP000260; ABF34698.1; -; Genomic_DNA.
DR RefSeq; WP_020905450.1; NC_008022.1.
DR AlphaFoldDB; Q1JF61; -.
DR KEGG; sph:MGAS10270_Spy1633; -.
DR HOGENOM; CLU_007524_0_1_9; -.
DR Proteomes; UP000002436; Chromosome.
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};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:ABF34698.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}.
FT DOMAIN 344..494
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 758..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 355..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 817 AA; 91491 MW; E7B2D9A1E2FA3D9B CRC64;
MEYVFTGTVD RIIFENQANF FKILLLAIED TDSDIDDFEI IITGTMADII EGDDYTFWGE
LTQHPKYGQQ LKLSRYQKIK PSSSGLVNYF SSDHFKGIGK KTAEKIIVLY GHNTIDHILE
DPSKLETISG LSKANRQAFV AKLKLNYGTE QLIAGLVELG LSNRFAFQAF EKYKEEALDL
VKENPYQLVE DLQGFGFKMA DALAENLGIE SDSPKRFRAA LLHCLLEESI NRGDTYVQAR
QLLDFAITLL EDARQVECDP AAVAEQLSEL IIEGKIKNSD TKLFDASLYF AEEGIANNIS
RLLDTPLSQS FSHDTIQTTI QAVQKDFAIT YDQVQQEAIT KALTSKVFLL TGGPGTGKTT
VIRGILQAYA NLHQIDLDKK DLPILLAAPT GRAARRMNEL TGLPSATIHR HLGLNGDNDY
QAMEDYLDCD LLIVDEFSMV DTWLANQLLG AINSTTQVII VGDSDQLPSV GPGQVLSDLL
KVNSLPQIAL QKIFRQSQES TIVNLADQMR RGILAADFRD KKADRSYFEA QAAFIPDMIQ
KIVLSAIKSG IPAEEIQILA PMYKGQAGIN HLNQLMQELL NPLQGQTEFL FNDTHFRKGD
KVLHLVNDAQ LNVFNGDIGY ITDLIPAKYT ESKQDELILD FDGSEVTYPR NEWLKLTLAY
AMSIHKSQGS EFQVVILPIT RQSGRLLQRN VIYTAITRSK SKLILLGEYT AFEYAIKHEG
DKRQTYLIER FQEQSDLASS QPNQELKSKE QTSLFSNTAT LEDDSQKSSS QSTNSNPTEN
SQSDNDDFRL TPENYSTIDS MIGLTESDIA LFFQKKS
//
