ID C5RAZ6_WEIPA Unreviewed; 1269 AA.
AC C5RAZ6;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
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 ECO:0000313|EMBL:EER74665.1};
GN ORFNames=HMPREF0877_1141 {ECO:0000313|EMBL:EER74665.1};
OS Weissella paramesenteroides ATCC 33313.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; Weissella.
OX NCBI_TaxID=585506 {ECO:0000313|EMBL:EER74665.1, ECO:0000313|Proteomes:UP000004528};
RN [1] {ECO:0000313|EMBL:EER74665.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33313 {ECO:0000313|EMBL:EER74665.1};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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:EER74665.1}.
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DR EMBL; ACKU01000014; EER74665.1; -; Genomic_DNA.
DR RefSeq; WP_002828748.1; NZ_GG697132.1.
DR AlphaFoldDB; C5RAZ6; -.
DR STRING; 585506.HMPREF0877_1141; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000004528; Unassembled WGS sequence.
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 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}; Reference proteome {ECO:0000313|Proteomes:UP000004528}.
FT DOMAIN 1..477
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 505..817
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 22..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1269 AA; 143833 MW; F634E0E539A147AB CRC64;
MKFTDSQSAA IKTKGRNVLV SASAGSGKTR VLVERVMQRL LAGENVNEFL IVTFTEAAAS
EMKERLEGAI RSELIASVGE QRQHLLKQLR LLNIANISTL HAFALRLIEQ YHYTIDLDPQ
FRLMDDAERT LVMLEVYNTL LEEQYANDNE QHAFATFAAQ FTTSTTDDRA LQEATFSLYD
FATARPDAVN WLDHLSDLYQ VDQEDFTSSQ FYQAQLKPQI LKELQGIVDR SAVLVAQAPD
TMDEAPAVNR LLNLQADETA YQQALTLVQN EANDWNTVQQ TIKHIDLMSW GVDTQGKRKN
FTKKHDPELK IAWDRVKDER EALKKRFTIV LEKYFVLDQA GLVLAIQGAG RVIDRLVKLT
KDFSTDFLTE KLRRKVLDFN DLEHFALQIV SQEKVKAELQ ERYTEIMVDE YQDTNQLQEA
ILHEITSGDN LFQVGDIKQS IYKFRQADPT LFAGKLATYP SDTISEVITL QENFRSQPNV
TNFINYIFAQ AMSRSLGDIE YTGEAELVAG ADYYPEELPK KAELLLYLDD ANQDESPADA
EVDAEADTLA SDAPYTKATG QIRLTALKIQ ELMQSKFEIF DRQAQKKRPV NYGDITILVP
TKGQNLDVLD VFREMNIPIM IDGTENYFQT TEISVIMSFL QVIDNPHQDI PLVAVLRSPL
YDIGENGLAL IRAQTPEEDF YTAVKNLAND DEIDTIGDIS PALVKNTQTQ VQRFLADLAV
FRDLAVQNQI VTLLWAIYNR TGWLDYVGGL PSGAQRQANL HALYDRASAY QKSSFVGLYQ
FINYVTQLQS HDKDLGEADA NVAQDSVSLM TIHHSKGLEF PIVFLLNATR TMISQRETQG
SIILDAQAGG GMNYVDLQHH LKLITPQHEY IAQVKRQNAY AEQLRVLYVA LTRAEQQLFI
VGAYDNVDKL WQTWQQSAGV TEWMLPDTVR LAGKSFMDLL GMTLIRHPQA PEQFAPLRGY
DVNDVMQFDE IRTKTPKNAF AFDLEVINTQ DLVNRVANYQ PLSDDIVDTK DVTETSAEEN
TDWQSVLQFA YPYETATRAT AYQSVSEIKR LFEDPDLAEG RQLLDRRLVT DDLAGLRMTD
EELPEPDFMQ ESATRLSSAA IGTATHLVMQ RLDLTKGVPT EVVIRTLIQQ LVNEKLIDDK
IAPLISVAKI GRFFNDSPLG KQMIQHADSL RREVPFSLLL DAKRLYRAFD GDDKVLVHGI
IDGYFQVDDE IWLFDYKTDH VSQQAATNIL TKRYAGQLNI YAQALVAMGL PMPKRFIYAI
NAEKLIRLS
//
