ADDB_ALKMQ
ID ADDB_ALKMQ Reviewed; 1149 AA.
AC A6TVN9;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B {ECO:0000255|HAMAP-Rule:MF_01452};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01452};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01452};
DE AltName: Full=ATP-dependent helicase/nuclease AddB {ECO:0000255|HAMAP-Rule:MF_01452};
GN Name=addB {ECO:0000255|HAMAP-Rule:MF_01452}; OrderedLocusNames=Amet_4176;
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF;
RX PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
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 AddB nuclease domain is not
CC required for chi fragment generation; this subunit has 5' -> 3'
CC nuclease activity. {ECO:0000255|HAMAP-Rule:MF_01452}.
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:0000255|HAMAP-Rule:MF_01452};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01452};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC -!- SUBUNIT: Heterodimer of AddA and AddB. {ECO:0000255|HAMAP-
CC Rule:MF_01452}.
CC -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01452}.
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DR EMBL; CP000724; ABR50257.1; -; Genomic_DNA.
DR RefSeq; WP_012065205.1; NC_009633.1.
DR AlphaFoldDB; A6TVN9; -.
DR SMR; A6TVN9; -.
DR STRING; 293826.Amet_4176; -.
DR PRIDE; A6TVN9; -.
DR EnsemblBacteria; ABR50257; ABR50257; Amet_4176.
DR KEGG; amt:Amet_4176; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR OrthoDB; 1283891at2; -.
DR Proteomes; UP000001572; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008409; F:5'-3' 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-EC.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 3.
DR Gene3D; 3.90.320.10; -; 1.
DR HAMAP; MF_01452; AddB_type1; 1.
DR InterPro; IPR014140; DNA_helicase_suAddB.
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 PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR02773; addB_Gpos; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; DNA damage; DNA repair; Exonuclease; Hydrolase; Iron;
KW Iron-sulfur; Metal-binding; Nuclease; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1149
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379148"
FT DOMAIN 1..276
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 273..586
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 786
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1105
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1108
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1114
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1149 AA; 134509 MW; 96D5C022027AE4F8 CRC64;
MAIRYIFGRA GRGKSYLALE EIKQKLQEEE DNKLFLLVPE QFTLQAERDL IRKQELTGMM
RAEVLSFTRL AHRVFSEVGG LTRVPINELG KNMILRKIAD ESLKELSIYQ SIAKQDGFIT
KLNELICEMK QHDITPTELT MELNEIEEET ILKRKLEDIT LLYQRFNNYL KGQYVDNEDH
VNLLIENIER VEFLEGAEIW IDGFQSFTPQ IIRVIEKLAQ KVANITITFT MELNAKEKDK
DLFHITQKTY LKVKTIAQKF NLDEEVINLD IEERKVLPKE KEIAHIEREF NTYPYKQYAD
EIANLEIFAG SNLYSEMENV AAQIIHLVRN RGYRWNDIAL VSGGLDQYSM ILKRVFEEYH
IPYFIDEKRS IMNNPMIELI LSSIEILSRG YQYEDVFSFL KTGFSDLTKD EVEQLENYVL
QYGIRGKAYS EPFTKGFEKK QIQQKDKEEG EKQIDEEKKE KYNELRMRFI APFAKFEKRI
YRKKKIGEIT KALFEFMKEL NIEDKLNQWI EELREEKYFE YVNENTQIWN KIMEIFDQLT
EILADESATL KEYGRILEAG FLACKVGVIP STIDQVLVGS IERSKSHDIK ALFVVGVNDG
VLPFGQEDGG ILLDHERESL VKKGISIGTT LESSLLEEQF MIYSAFSKPT EYLWVSYALA
DQEGKAMRQS ILIDRFKKLF KNLRIKSDVV NDVDRQLHLI TTPISTFKYM TENIRQNVDD
KAMADMWWDV YDWYSKEPTW EDRRKLMVKG LFHQNQITYI GENKAKSLYD NPIKSSVSRL
ERFANCPFSH FVTYGLRPKE RKEYQLSNPD IGRLFHDSME QFTKEMVNEE IQWKDLTKEK
NDELVEKVID EMVPDFEHGI MLSTHRYQYL VTRLKRISKR AMWTLTDHVK KGEFVPMGHE
IIFGLEGDVP PIIIELANGE KIYLEGRIDR VDLLNDEEDG NYVKIIDYKS GSKEFSLSDV
YYGLQIQLMV YLDAILSSEE KKHQVEIHPG GIFYFKIDDP MVKTTEKVVE EVEKEINKKL
KMKGLVLKDV NIIKKMDRSI GRSSTIVPAG LTKDDEISKS SSALPEEDFK ALLNHVRRLV
KEIGEEMLKG NVKIEPFKKG GDTSCKYCDY IAICQFDNSF HDNQYKNIKE LKSDEVLERI
KKESQKKLE
