EX7L_CHLMU
ID EX7L_CHLMU Reviewed; 516 AA.
AC Q9PK65;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE EC=3.1.11.6 {ECO:0000255|HAMAP-Rule:MF_00378};
DE AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE Short=Exonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
GN Name=xseA {ECO:0000255|HAMAP-Rule:MF_00378}; OrderedLocusNames=TC_0605;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
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).
CC -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large acid-
CC insoluble oligonucleotides, which are then degraded further into small
CC acid-soluble oligonucleotides. {ECO:0000255|HAMAP-Rule:MF_00378}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-
CC direction to yield nucleoside 5'-phosphates.; EC=3.1.11.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00378};
CC -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00378}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00378}.
CC -!- SIMILARITY: Belongs to the XseA family. {ECO:0000255|HAMAP-
CC Rule:MF_00378}.
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DR EMBL; AE002160; AAF39436.1; -; Genomic_DNA.
DR PIR; B81684; B81684.
DR RefSeq; WP_010230965.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PK65; -.
DR SMR; Q9PK65; -.
DR STRING; 243161.TC_0605; -.
DR EnsemblBacteria; AAF39436; AAF39436; TC_0605.
DR GeneID; 1245967; -.
DR KEGG; cmu:TC_0605; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_0; -.
DR OMA; KIACTIW; -.
DR OrthoDB; 1371775at2; -.
DR Proteomes; UP000000800; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009318; C:exodeoxyribonuclease VII complex; IEA:InterPro.
DR GO; GO:0008855; F:exodeoxyribonuclease VII activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006308; P:DNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd04489; ExoVII_LU_OBF; 1.
DR HAMAP; MF_00378; Exonuc_7_L; 1.
DR InterPro; IPR003753; Exonuc_VII_L.
DR InterPro; IPR020579; Exonuc_VII_lsu_C.
DR InterPro; IPR025824; OB-fold_nuc-bd_dom.
DR PANTHER; PTHR30008; PTHR30008; 1.
DR Pfam; PF02601; Exonuc_VII_L; 2.
DR Pfam; PF13742; tRNA_anti_2; 1.
DR TIGRFAMs; TIGR00237; xseA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease.
FT CHAIN 1..516
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000197835"
SQ SEQUENCE 516 AA; 58883 MW; F8BF029768026EB1 CRC64;
MSITSPPVEV SVLTDSIKNL LEKNFLRVVV KGELSNVSLQ TSGHLYFAIK DSKAVLNGAF
FHFRSKYFDR RPKDGDYVIL HGKLTVYAPR GQYQIVAYAL TFSGEGNLLQ QFEERKQRLA
AEGYFDPKRK RQIPSEARTI GVITSPTGAV IQDILRVLSR RCHQFQVILY PVTVQGPTAA
QEISRAIQVF NQENIKIDTL IVARGGGSIE DLWAFNEEIL VKAIAASSIP IISAVGHETD
FTLCDFAADV RAPTPSAAAE IVCKSSEQYH QELQNLLRHL SSHSRQFIAA KKNLLSHWKK
HLATADFYHT AQQTLDYTRL SLERTLDAKL EHYKQHLAQY KRWLKSDILI RVEKHLSNLN
QALESAIKNK LYSNKVSLHQ LYTSRFKNEL PNLQHRTQHA KHLLNQLSRR LHFVMANSQE
TKLQRFARLQ EEFSFMIQHL LTKAKERCQS VQEQMASLNP KNVLKRGFAQ LFDFNKHSVI
ISAESLKQSD LVRVCLQDGE AVLSVKEVWL NNDKKG