ID EX7L_STAS1 Reviewed; 445 AA.
AC Q49XW8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 112.
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=SSP1231;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE18376.1; -; Genomic_DNA.
DR RefSeq; WP_011303037.1; NZ_MTGA01000038.1.
DR AlphaFoldDB; Q49XW8; -.
DR SMR; Q49XW8; -.
DR KEGG; ssp:SSP1231; -.
DR PATRIC; fig|342451.11.peg.1230; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_9; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000006371; 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 NCBIfam; TIGR00237; xseA; 1.
DR PANTHER; PTHR30008; EXODEOXYRIBONUCLEASE 7 LARGE SUBUNIT; 1.
DR PANTHER; PTHR30008:SF0; EXODEOXYRIBONUCLEASE 7 LARGE SUBUNIT; 1.
DR Pfam; PF02601; Exonuc_VII_L; 1.
DR Pfam; PF13742; tRNA_anti_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome.
FT CHAIN 1..445
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000197886"
SQ SEQUENCE 445 AA; 51170 MW; 0A4441684051E000 CRC64;
MSEYLSVTSL TKYIKYKFDQ DPHLQSVLIK GELSNFKKHS SGHLYFNVKD KNSVISAMMF
KGNASKIDFE PKEGDEVLLE ARVSVYERRG NYQIYVNKMH MDGIGNLYQK LEQLKKKLTK
EGFFDQNHKK VIPKFPQKIA VLTAGTGAAI RDIHTTINSR YPLAEQVQIN TLVQGEQAKS
DIIEKINQAD ALNVDTIIIG RGGGSIEDLW NFNEEDVVKA IYNCQTPIIS AVGHETDFTL
SDFVADVRAA TPTQAAVMAT PDQYELRQYL QQANLSLTRF IKQYMQQKRK HLEHVASYYK
FQTPSLLYDQ QIQKRDDLEK QLKLSLNLKI KNQQQQLQLL FNNFNLKTFK QRIKRDQLTN
NQKRVELSKV MHNLLDNQKN NLARKLENLN NLSPTNTMLR GYTIVNKDDK VITSTKDLAE
NDNIVLTMKD GVVDAQVKKV RCNDE
//
