RECB_CHLPN
ID RECB_CHLPN Reviewed; 1050 AA.
AC Q9Z7G7; Q9JSB1; Q9K2F2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=RecBCD enzyme subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
DE EC=3.1.11.5 {ECO:0000255|HAMAP-Rule:MF_01485};
DE AltName: Full=Exonuclease V subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
DE Short=ExoV subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
DE AltName: Full=Helicase/nuclease RecBCD subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
GN Name=recB {ECO:0000255|HAMAP-Rule:MF_01485};
GN OrderedLocusNames=CPn_0738, CP_0007, CpB0767;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for
CC recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly
CC rapid and processive ATP-dependent bidirectional helicase activity.
CC Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator)
CC sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the
CC Chi site. The properties and activities of the enzyme are changed at
CC Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and
CC facilitates RecA-binding to the ssDNA for homologous DNA recombination
CC and repair. Holoenzyme degrades any linearized DNA that is unable to
CC undergo homologous recombination. In the holoenzyme this subunit
CC contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA
CC onto ssDNA. {ECO:0000255|HAMAP-Rule:MF_01485}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage (in the presence of ATP) in either
CC 5'- to 3'- or 3'- to 5'-direction to yield 5'-
CC phosphooligonucleotides.; EC=3.1.11.5; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01485};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01485};
CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC to DNA-binding. Interacts with RecA. {ECO:0000255|HAMAP-Rule:MF_01485}.
CC -!- DOMAIN: The N-terminal DNA-binding domain is a ssDNA-dependent ATPase
CC and has ATP-dependent 3'-5' helicase function. This domain interacts
CC with RecC. {ECO:0000255|HAMAP-Rule:MF_01485}.
CC -!- DOMAIN: The C-terminal domain has nuclease activity and interacts with
CC RecD. It interacts with RecA, facilitating its loading onto ssDNA.
CC {ECO:0000255|HAMAP-Rule:MF_01485}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01485}.
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DR EMBL; AE001363; AAD18877.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF37903.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98945.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98695.1; -; Genomic_DNA.
DR PIR; C81624; C81624.
DR PIR; G86582; G86582.
DR PIR; H72041; H72041.
DR RefSeq; NP_224934.1; NC_000922.1.
DR RefSeq; WP_010895365.1; NZ_LN846995.1.
DR AlphaFoldDB; Q9Z7G7; -.
DR SMR; Q9Z7G7; -.
DR STRING; 115711.CP_0007; -.
DR EnsemblBacteria; AAD18877; AAD18877; CPn_0738.
DR EnsemblBacteria; AAF37903; AAF37903; CP_0007.
DR GeneID; 45050793; -.
DR KEGG; cpa:CP_0007; -.
DR KEGG; cpj:recB; -.
DR KEGG; cpn:CPn_0738; -.
DR KEGG; cpt:CpB0767; -.
DR PATRIC; fig|115713.3.peg.814; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_6_3_0; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 3.
DR Gene3D; 3.90.320.10; -; 2.
DR HAMAP; MF_01485; RecB; 1.
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; IPR004586; RecB.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070; PTHR11070; 2.
DR PANTHER; PTHR11070:SF23; PTHR11070:SF23; 2.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR00609; recB; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleotide-binding.
FT CHAIN 1..1050
FT /note="RecBCD enzyme subunit RecB"
FT /id="PRO_0000102044"
FT DOMAIN 1..443
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT DOMAIN 458..701
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT REGION 1..800
FT /note="DNA-binding and helicase activity, interacts with
FT RecC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT REGION 814..1050
FT /note="Nuclease activity, interacts with RecD and RecA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT ACT_SITE 958
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 21..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 859
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 945
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 958
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT CONFLICT 142
FT /note="N -> K (in Ref. 2; AAF37903)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="V -> I (in Ref. 1; AAD18877)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1050 AA; 121056 MW; 6E2CD03C2AEB83B7 CRC64;
MKPFNIFDSN SSIQGKFFLE ASAGTGKTFT IEQIVLRALI EGSLTHVEHA LAITFTNAST
NELKVRIKDN LAQTLRELKA VLNSQPASLP TYLDINCNVK QIYMQVRNAL ATLDQMSLFT
IHGFCNFVLE QYFPKTRLIH KNPALTHSQL VLHHITNYLK QDLWKNVLFQ EQFHLLAVRY
NVTSKHTSSL VDKLLASYTQ PISSYFSSRV ERLEQISLWH QQIYNSLLEI PKQVFLDQLT
AHISGFKKQP FSILDDLHHF VDLLYTSETH SSLFSFFKIA ETFNFKHRLA RYKPCAAFTV
LENMSWVERT LEFCNLDRIF NTLLVDLQEY LKQNYTPWLS PDESVFALEK LLSSSEAQPV
VQALREQYQL VLIDEFQDTD KQQWSIFSNL FISPKFTGSL FLIGDPKQSI YEWRSADLPT
YLTAKSSFSE DKQLQLVNNY RSTPKLMEAI NQIFGKISPF LEIPGYLPIE YHALNPQSSE
TFENPPHAPI HFFFYETIKD QALWIFSEAL RLQKEQKIPL GNMVVLVSDS NQAFELISYA
TIPVSFSKNK SIFHLTETHI LTTALLEAIL HPENYEKISK ILFSSLFGLS LDEVTTKKED
FTIYFQSLHS YISHHGLLAT FYRVMTTQGN VLFSSPRGDL IFQEMEKLCG YLDTISSYPY
HQLLHLKNFS ETGRWEEELA ISSYSEDLET LKITTIHSSK GLEYDIVFCP GIEKSKKNKS
SSELLREMYV ACTRAKKQLY LPISTQPPSL QRSSALTNYV KLEGTQSSAY DLAIHLHQEH
PDLFSYSLPK DHGHATTVLN LPLLETFALK VTPPKTIFSF SSTKFLLDTH KDSQSIPYSK
LPISKQQLPL GEKTGILIHK ILESIQFSLL QDTEYLMSTI MRFIKHTHLE GFEETILKLL
SKTFFSPLTF SSQTFSLSQV LPNKIFRETS FLFLENQELW QGVIDLFFEH EGKYYIIDWK
TSFLGETNSD YSKSNLSIYI KQEKLDYQGR IYVKAVRKFL NQFEIDDDVE LGVIFIRGID
TQGNGFFALN SSEDIPNFNP KAIQKCQAYH
