ADDB_RUMCH
ID ADDB_RUMCH Reviewed; 1149 AA.
AC B8I2Y3;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Ccel_1775;
OS Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS H10) (Clostridium cellulolyticum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminiclostridium.
OX NCBI_TaxID=394503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Zhou J., Richardson P.;
RT "Complete sequence of Clostridium cellulolyticum H10.";
RL Submitted (JAN-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 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; CP001348; ACL76126.1; -; Genomic_DNA.
DR RefSeq; WP_015925241.1; NC_011898.1.
DR AlphaFoldDB; B8I2Y3; -.
DR SMR; B8I2Y3; -.
DR STRING; 394503.Ccel_1775; -.
DR PRIDE; B8I2Y3; -.
DR EnsemblBacteria; ACL76126; ACL76126; Ccel_1775.
DR KEGG; cce:Ccel_1775; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR OrthoDB; 1283891at2; -.
DR Proteomes; UP000001349; 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 PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02773; addB_Gpos; 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_0000379176"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 788
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1106
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1109
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1115
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1149 AA; 132140 MW; 3A6E6F958CCA51CE CRC64;
MGLQFIYGRA GSGKSFHCLN SIKTKQNKDS NKKLVLIVPE QYTLQAERDL IKVLGTGGIL
KTEVLSFRRM AYRVLNEVGG ITYPHIHPSG KNMIIYRILE RLKDQFTIFH KSANCKGFVN
TLSTLITELK RYNVRAESFD EVLQGLADDN YLSHKLKEIK LIYSEFDSML VDRYRDTDDE
LTLLSSKLEG TEIYAKSEIW IDGFAGFTPQ EVEVISKLIQ QAENVHITMC TDILFDDVQA
DLTDVFAAVK KSCKKFVSIA ESYGVKILPP VCLNTPNLPR FKDSRELQSL ETNYCSYSYR
AYQLPTQDIE LFESVNIYTE IEECARDIIK QCRDNGMQFK DITVATRNLT GYENLIGVIF
EQYNIPCFID SKTEITNHPL VRMVLSMLEI FTENWSYESV FRYLKSGLTG IDNTKIDILE
NYVLACGIRG SRWTQEADWN TSIEFRPDDG QKPENDEMLL NINKTRNEIR EPLIRFRNRT
KGRRTAGDFC AGIYEYLVEI GVEQRIRNYI EKFTQSGQLR LAGEYQQVWN ILMDVFDQAV
EVMADETFGL EKFANVFKIG LAEYKISSIP ASLDQVLVGS IEHIRSHEIK ALYILGTNDG
VFPSAGMSEG VLSDADREVL DKRGIELASD TKTRAFDEQY LIYRTLTTPK NYLRLSWPIA
DHEGRTMRPS TIISRMRKIF PKVTEKSNIV KPSADKQHID LIASPIPAFN QLVCALRQKN
EGIEQGEIWR EIFAWFSGQD EWKQKCDAMI NALKYRNIAA PVDKSKIREL YGKSPYFTVS
RLEKYTSCPF AFYVQYGLGA RERKIYRMSP PDVGTFMHAV IERFSKMVDE NNYSWREFDR
QWCSEQVSKI VDELLDSMKN TILGGSKRFK ALAVRLKRVV TRAVWLITEH IRRSSFEPVG
YEVDFGDGGA YPPMVIELDS GEKIRLVGRI DRIDALRAEN GTYLRIVDYK SGEKDFKLSD
VYYGLQMQLI TYLDALWEYS DKSNGEKIIP GGILYFRIDD PMIRCTDNST PEEIETAIMK
KLKMKGLLLA DVQLIKYMDN TIEGNSIIIP ARINKGDVLG KSSAATIEQF TVLRSYVKQL
LKDMCSELMK GNVPISPYKK KKLTSCSYCN YSSVCQFDQS QKENSFRMLH DREDNDIWKL
MNEIDVKDN
