ID S5RHD4_9STRE Unreviewed; 1208 AA.
AC S5RHD4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=ATP-dependent helicase/nuclease subunit A {ECO:0000256|HAMAP-Rule:MF_01451};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01451};
DE EC=5.6.2.4 {ECO:0000256|HAMAP-Rule:MF_01451};
DE AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000256|HAMAP-Rule:MF_01451};
DE AltName: Full=DNA 3'-5' helicase AddA {ECO:0000256|HAMAP-Rule:MF_01451};
GN Name=addA {ECO:0000256|HAMAP-Rule:MF_01451};
GN ORFNames=KE3_0700 {ECO:0000313|EMBL:AGS05206.1};
OS Streptococcus lutetiensis 033.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1076934 {ECO:0000313|EMBL:AGS05206.1, ECO:0000313|Proteomes:UP000015268};
RN [1] {ECO:0000313|EMBL:AGS05206.1, ECO:0000313|Proteomes:UP000015268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=033 {ECO:0000313|EMBL:AGS05206.1,
RC ECO:0000313|Proteomes:UP000015268};
RX PubMed=23782707; DOI=10.1186/1471-2180-13-141;
RA Jin D., Chen C., Li L., Lu S., Li Z., Zhou Z., Jing H., Xu Y., Du P.,
RA Wang H., Xiong Y., Zheng H., Bai X., Sun H., Wang L., Ye C., Gottschalk M.,
RA Xu J.;
RT "Dynamics of fecal microbial communities in children with diarrhea of
RT unknown etiology and genomic analysis of associated Streptococcus
RT lutetiensis.";
RL BMC Microbiol. 13:141-141(2013).
CC -!- FUNCTION: The heterodimer acts as both an ATP-dependent DNA helicase
CC and an ATP-dependent, dual-direction single-stranded exonuclease.
CC Recognizes the chi site generating a DNA molecule suitable for the
CC initiation of homologous recombination. The AddA nuclease domain is
CC required for chi fragment generation; this subunit has the helicase and
CC 3' -> 5' nuclease activities. {ECO:0000256|HAMAP-Rule:MF_01451}.
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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618, ECO:0000256|HAMAP-
CC Rule:MF_01451};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01451};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01451};
CC -!- SUBUNIT: Heterodimer of AddA and AddB/RexB. {ECO:0000256|HAMAP-
CC Rule:MF_01451}.
CC -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01451}.
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DR EMBL; CP003025; AGS05206.1; -; Genomic_DNA.
DR RefSeq; WP_020916501.1; NC_021900.1.
DR AlphaFoldDB; S5RHD4; -.
DR KEGG; slu:KE3_0700; -.
DR PATRIC; fig|1076934.5.peg.640; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR Proteomes; UP000015268; Chromosome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; 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:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR HAMAP; MF_01451; AddA; 1.
DR InterPro; IPR014152; AddA.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR NCBIfam; TIGR02785; addA_Gpos; 1.
DR PANTHER; PTHR11070:SF48; ATP-DEPENDENT HELICASE_NUCLEASE SUBUNIT A; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01451};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01451};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01451};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01451};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01451}.
FT DOMAIN 26..482
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 510..798
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 47..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1208 AA; 138418 MW; 0D6E2C405BD59F90 CRC64;
MTFKPFLTAE AISSLQQKEA QSSKAQKRTP EQIEAIYSYG NNILVSASAG SGKTFVMVER
IIDKILRGIT VDQLFISTFT VKAAGELKER LEKKISQALQ QATHNDLKNY LNEQLLALQT
ADIGTMDAFT QKLVNQYGYT LGISPTFRIM TDKSEQDLVK NDVFADLFAD YMTGQNQDIF
RKLVRNFSGN RKDTTAFRGI VYKIYDFSQA TDNPKKWLTE VFLKGARTYT DFSAIPDQEV
VDFLACMHET ANQLQDVTDL EDYKQKTAKG TPTAAYKRHL NMIEHLHEWA LHFETLYGRD
GLGRLATDVA DLIPSSPAVT VAGVKYPIFK TLQGRLAGLK HLETIFKYQS ESLPLLELLQ
AFMQDFSEQY LQAKIQENAF EFSDIAHFAI QILEENPDIR ELYQDKYHEV MVDEYQDNNH
TQERMLELLS NGHNRFMVGD IKQSIYRFRQ ADPQIFNQKF KDFQEHPEHG KLILLKENFR
SQSEVLDTTN SVFTHLMDES VGEILYDGMH QLVAGSPAQK EAHPENKTQV LIYDTDDGGE
LASSPEEEQI NPNEVKLVAK EIIRLHNEEG VAFEDITLLV SSRTRNDGIL QTFEHYGIPL
VTDGGEQNYL KSVEVMVMLD TLRALDNPLN DYALVALMRS PMFSFNEDDL ARLALQTSED
ETRANLYQKL EHALANQGQH AELVTLVLRE KLKDFMTCFS KWRDFAKWHS LYDLIWKIYN
ERFYYDYVGN LPRAEQRQAN LYALALRANN FEKTGFKGLS RFIRMIDRVL ESENDLADVE
VALPKHAVNL MTIHKSKGLE FKYVFILNID KKFSIQDMMS PLILSRQNGA GIKYLADMRE
ELDTDVFPTV KVSMDTLPYQ LNKRELRLAT LSEQMRLFYV AMTRAEKKLY LVGKASSEKL
VDKYSGKSEN NHLPVAEREA FMTFQDWMLA IHEAYKDLPF KVEFVTDEDL TEEKIGQIEV
KSAIKPDDLS NNRQSENIAE ALERLEAVAE LNTKYQSAIN LPSLRTPSQV KKLYELVMDT
DGVDVMAKKD QVKPSFALPD FSKKAKVEAT AIGSAMHELM QRISLSQKVT LEDISKALTQ
VSAKDEVKAR IHLENVLDFF ENSALGQLIQ QNTDKIYREA PFAMLKEDPE SKEKFVVRGI
VDAYLILEDR LVLLDYKTDK YTNSEEIKDR YQGQMALYAE ALSKSYHIDQ VDKYLVLLGG
ECLEVVKL
//
