EX7L_STRZP
ID EX7L_STRZP Reviewed; 446 AA.
AC C1CKV3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 71.
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=SPP_1248;
OS Streptococcus pneumoniae (strain P1031).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=488223;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1031;
RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA Rappuoli R., Moxon E.R., Masignani V.;
RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT closely related species.";
RL Genome Biol. 11:R107.1-R107.19(2010).
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; CP000920; ACO20528.1; -; Genomic_DNA.
DR RefSeq; WP_000417464.1; NC_012467.1.
DR AlphaFoldDB; C1CKV3; -.
DR SMR; C1CKV3; -.
DR KEGG; spp:SPP_1248; -.
DR HOGENOM; CLU_023625_3_1_9; -.
DR OMA; WPAVRFE; -.
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; 1.
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..446
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000200684"
SQ SEQUENCE 446 AA; 50508 MW; 843E048235BBB986 CRC64;
MEKYLSVTTL TKYLKMKFDK DPYLERVYLT GQVSNFRKRP THQYFSLKDD HAVIQATIWS
GIYQKLGFDL EEGMKINVIG RVQVYEPSGS YSIIIEKAEP DGVGALAIQF EQLKKKLTEE
GLFQERFKQA LPQFSKRIGV VTSRSGAVIR DIITTVSRRF PGVDILLYPT KVQGEGAAEE
IARNIARANQ RDDLDLLIIG RGGGSIEDLW AFNEEIVVRA IFESRLPVIS SVGHETDVTL
ADFVADRRAA TPTAAAELAT PVTKLDVLAH LQNQEKRMVT AVRNVLSKKQ EALKKCSQSV
IFRQPERLYD GYLQRLDQLQ LRLKQSLRTR ISDNKQLVQA RTHQLVQLSP VTKIQRYQDR
LGQLDKLLGS QMALVYDAKV AEAKRLSEAL LMLDTSRIVA RGYAIVKKEE SVVDSVESLK
KKDQVTLLMR DGQVELEVKD VKTKEI
