ID A0A2M8TFL3_9CLOT Unreviewed; 1153 AA.
AC A0A2M8TFL3;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B {ECO:0000256|HAMAP-Rule:MF_01452};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01452};
DE EC=5.6.2.4 {ECO:0000256|HAMAP-Rule:MF_01452};
DE AltName: Full=ATP-dependent helicase/nuclease AddB {ECO:0000256|HAMAP-Rule:MF_01452};
DE AltName: Full=DNA 3'-5' helicase AddB {ECO:0000256|HAMAP-Rule:MF_01452};
GN Name=addB {ECO:0000256|HAMAP-Rule:MF_01452,
GN ECO:0000313|EMBL:PJI09771.1};
GN ORFNames=CUB90_18700 {ECO:0000313|EMBL:PJI09771.1};
OS Clostridium sp. CT7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=2052574 {ECO:0000313|EMBL:PJI09771.1, ECO:0000313|Proteomes:UP000230839};
RN [1] {ECO:0000313|EMBL:PJI09771.1, ECO:0000313|Proteomes:UP000230839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT7 {ECO:0000313|EMBL:PJI09771.1,
RC ECO:0000313|Proteomes:UP000230839};
RA Xin F., Chen T.;
RT "The draft genome sequence of Clostridium sp. CT7, a unique bacterium
RT capable of producing butanol from glycerol uncoupled acetone and 1,3-
RT propanediol formation.";
RL Submitted (NOV-2017) 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:0000256|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=5.6.2.4;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01452};
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_01452};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01452};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01452};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_01452};
CC -!- SUBUNIT: Heterodimer of AddA and AddB. {ECO:0000256|HAMAP-
CC Rule:MF_01452}.
CC -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01452}.
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:PJI09771.1}.
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DR EMBL; PETE01000002; PJI09771.1; -; Genomic_DNA.
DR RefSeq; WP_066022629.1; NZ_PETE01000002.1.
DR AlphaFoldDB; A0A2M8TFL3; -.
DR OrthoDB; 9758506at2; -.
DR Proteomes; UP000230839; Unassembled WGS sequence.
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-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: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; 3.90.320.10; -; 1.
DR Gene3D; 6.10.140.1030; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR HAMAP; MF_01452; AddB_type1; 1.
DR InterPro; IPR049035; ADDB_N.
DR InterPro; IPR014140; DNA_helicase_suAddB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR NCBIfam; TIGR02773; addB_Gpos; 1.
DR PANTHER; PTHR30591; RECBCD ENZYME SUBUNIT RECC; 1.
DR PANTHER; PTHR30591:SF1; RECBCD ENZYME SUBUNIT RECC; 1.
DR Pfam; PF21445; ADDB_N; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01452};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01452}; DNA damage {ECO:0000256|HAMAP-Rule:MF_01452};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01452};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01452}; Helicase {ECO:0000313|EMBL:PJI09771.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01452};
KW Iron {ECO:0000256|HAMAP-Rule:MF_01452};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01452};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01452};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01452};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01452};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01452}; Reference proteome {ECO:0000313|Proteomes:UP000230839}.
FT DOMAIN 5..287
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21445"
FT DOMAIN 775..1114
FT /note="PD-(D/E)XK endonuclease-like"
FT /evidence="ECO:0000259|Pfam:PF12705"
FT BINDING 786
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1104
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1107
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1113
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1153 AA; 133760 MW; 16A967BCAA1F5D6F CRC64;
MSLRFIYGRA GSGKSQFCIN SIHSRIEKGG DKPLILVVPE QFSFQSEKSI LTLIGEKSLS
RVRVISFKRM AYRVFDEVGG IAREHMNSSG KSMLFYHIMN KLKDEFKVFA LSARQKGFVD
TVSDTISEFK KYELTPEILR STIDNVEDDE LKNKLHDLSL IYDEFDKLLH KNYIDSDDDL
TMLKDKIKFS NMLSGAEIWL DEFSSFIPQQ YGIIEELLKK CSRVNITLTM DYGNVPYDDD
IFSVTKNTEN RIMKIAQDNN VKIDKPVNLN KRPFYRFKRS PELGFLEKNL YSFPYEIYKS
EPKKIGIFKT SNLYTEVEET ARKIVEFVRD KKMRYSDMAV VTGDLGSYKK TVAVIFKEYG
IPFFIDENKD IEDNTLIILI KSIMDIFIKN WSYEAVFRYL KTGFTDVPYD DIDILENYVL
AAGIKGKKKW TEKDWTYNVY HNGYDDEVSV ENQERLAKVN EIRNKVVEPI VEFRKKVLRK
SNVAEICKSL FEFLCDINVP DKVEKMVSEF RESGRQVLAN EYSQIWNVII ELMDQLVEVM
GDEKANLEQF SKIFSIGVKE HKMGLIPSSL DQVLVGSIDR LKSHAIKLIF IMGVNDGVFP
SAAMEEGILS DRDREILMNS GVELAKDTKT QAMEQRFLVY TSIANSSEYL ILSYPIADYE
GKTLRPSMII NRMKTLFPEL KEKSDVIKID NDDENMKLVS STVPTFNEMV ASFRKEVDGK
NHSSAVWHDV YRWYCKDESW SQKCSNMFKA VAYTTQVDYI SEEKAVKLYG SSLKMSVSRL
EKYVECPFSY YVQYGLNIKE RKMFSLTPPD LGSFMHKVID EFCENIREEN IEWKDVDDKV
CEKKIYEIVD RELEDNAGSI FNSSPRYSYM TLRLKRILKR TARIVAEQFK RSGFRPAGYE
VTFENGGNYP PITVKLADNS EVVLTGRIDR IDMLEKDGNT YIRIIDYKSG NKIFKLSDVY
YGFDIQLLLY LDAILQSENL EDDDRTLPGG IFYFTMDDPI IKDKRNLTEE EIKEEIMKHL
KMKGLLLSDP EVVHEMDRQM EGASILIPAS IKKDGTLGRS SAATKEQFEM LIGHVKNLVI
KNCEKLLMGD IKIRPYKNGK EKPCDYCIYS SICRFDTMFH GNNYRYVKEK SDDEVFKLIG
KEIDEEGDYN ERN
//