EX7L_CHLTA
ID EX7L_CHLTA Reviewed; 516 AA.
AC Q3KM31;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=CTA_0356;
OS Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=315277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT genitotropic strains.";
RL Infect. Immun. 73:6407-6418(2005).
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; CP000051; AAX50591.1; -; Genomic_DNA.
DR RefSeq; WP_009872565.1; NC_007429.1.
DR AlphaFoldDB; Q3KM31; -.
DR EnsemblBacteria; AAX50591; AAX50591; CTA_0356.
DR KEGG; cta:CTA_0356; -.
DR HOGENOM; CLU_023625_3_1_0; -.
DR OMA; KIACTIW; -.
DR Proteomes; UP000002532; 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_0000303780"
SQ SEQUENCE 516 AA; 58605 MW; 99585B23C1222DA5 CRC64;
MSITSPPIEV SVLTDSIKNL LEKNFLRVVV KGELSNVSLQ TSGHLYFAIK DSKAVLNGAF
FHFRSKYFDR KPKDGDYVIL HGKLTVYAPR GQYQIVAYAL TFSGEGNLLQ QFEERKQRLA
AEGYFDPKRK KPLPSGARVI GVITSPTGAV IQDILRVLSR RCHQFQVILY PVTVQGATAA
QEISQAIQFF NQNSMGVHAL IIARGGGSIE DLWAFNEEEL VKSIVASSIP IISAVGHETD
FTLCDFASDV RAPTPSAAAE IVCKSSDQYR QELQNLRRYV SSHARQFIAA KKNLLTHWQR
HLASVDFYHT AQQTLDYTRA ALERGIETKL EYYKQRFAQY RRWLKSDVLI RIEKHLADLN
QSLMLSIKNK IYTKKTSLNQ LYTSCLKNEL LNLQHRTQHS RNILSQLSRR LHIAIASSQQ
THQECLVRLQ NELSFTIQHL LTKAKERCQA IQEQASSLNP KNVLKRGFAQ LFDFNKHFVI
ISAESLKQSD LVRVCLQDGE AVVSVKEVWL NNDKKG
