ID B9E6Z8_MACCJ Unreviewed; 796 AA.
AC B9E6Z8;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
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=recD2 {ECO:0000256|HAMAP-Rule:MF_01488};
GN OrderedLocusNames=MCCL_1259 {ECO:0000313|EMBL:BAH17966.1};
OS Macrococcus caseolyticus (strain JCSC5402).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX NCBI_TaxID=458233 {ECO:0000313|EMBL:BAH17966.1, ECO:0000313|Proteomes:UP000001383};
RN [1] {ECO:0000313|EMBL:BAH17966.1, ECO:0000313|Proteomes:UP000001383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC5402 {ECO:0000313|EMBL:BAH17966.1,
RC ECO:0000313|Proteomes:UP000001383};
RX PubMed=19074389; DOI=10.1128/JB.01058-08;
RA Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL J. Bacteriol. 191:1180-1190(2009).
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; AP009484; BAH17966.1; -; Genomic_DNA.
DR RefSeq; WP_012657164.1; NC_011999.1.
DR AlphaFoldDB; B9E6Z8; -.
DR STRING; 458233.MCCL_1259; -.
DR KEGG; mcl:MCCL_1259; -.
DR eggNOG; COG0507; Bacteria.
DR HOGENOM; CLU_007524_0_1_9; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000001383; 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; PF13604; AAA_30; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}; Reference proteome {ECO:0000313|Proteomes:UP000001383}.
FT DOMAIN 351..508
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 362..366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 796 AA; 90333 MW; E83A57C736911DA2 CRC64;
MENMTLFEQS FVKGTITRIL FYNNDNFYTV LKAEVIESNE DFDDDATITG YLPQIAEGDT
YTFTGKIITH PKYGKQLQAD KFEKDMPQSR DGIIHYLSSD LFKGVGKKTA RTIVEVLGED
ALNIILDDKS SLDQVPKLSD EKKELIYSTI HDNQAIEKIM IQLNEFGFGP QLAMKIYQFY
KDDTLKVINE SPYQLVMDIE GIGFNKADEL AGKLGIDNNH PERLKAALVF TIEQASNQNG
HTYIPDQVLL ETSFNLLTKN GSQVNPDRLV IALTELTEEH KLVEHEKNIY IPSLFYSETK
AVQILHRLMN HKNQVKEFEQ SEVLMAIGEL EALFEVSYAE RQKDALITAM NSKLMILTGG
PGTGKTTVVR GIVNLYAELH GLSLDYDDYD GQDYPIVVAA PTGRASKRLQ ESTGLEATTI
HRLIGWTKEN KPDDVLETEI TAKLVIIDEM SMVDTWLMFQ LMKAVPDDAQ IIFVGDQDQL
PSVGPGQVFK DMIDAHIMPQ IELNEVYRQQ EGSSIVELAH QIKRNEPFDI KKRYNDRSFI
PCTSNQIPEV IEKIVRSAVN KGYDMRDIQV LAPIYRGPAG IRALNKVLQE ILNPSDENKR
ELQFGDVYFR TGDKVLQLVN RPEDNVFNGD IGEVTGIFMA AENALNKDVV IVDYDGSEVT
YTKADLMEIT HAYCCSIHKS QGSEFPIVIM PVVNQYYRML QKNILYTGLT RAKQSLIFCG
DVHAFNEGIK RIGNTRFTSF YQFLIDYFNE DEINDKKQDD QGNILPFNVG EMTEDNMHLV
DPMINMEGIT PYDFIS
//
