EX7L_BARHE
ID EX7L_BARHE Reviewed; 475 AA.
AC Q6G2I3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=BH12220;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897699; CAF28004.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6G2I3; -.
DR SMR; Q6G2I3; -.
DR STRING; 283166.BH12220; -.
DR PaxDb; Q6G2I3; -.
DR PRIDE; Q6G2I3; -.
DR EnsemblBacteria; CAF28004; CAF28004; BH12220.
DR KEGG; bhe:BH12220; -.
DR eggNOG; COG1570; Bacteria.
DR OMA; WPAVRFE; -.
DR Proteomes; UP000000421; 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; 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..475
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000122043"
SQ SEQUENCE 475 AA; 53448 MW; 64DC680DB77012B4 CRC64;
MNLFFEKTGA TNVAEFSVSE IAGALKRVVE EKFGYVRVRG EISGYRGAHA SGHAYFALKD
DKARLEAVIW RGIMEKLKFP PEEGMEVIAV GKLTTYPGSS KYQIVIEALE PTGVGALMTL
LENRKKKFAE EGLFDEEKKK PLPYMPKIIG VVTSPTGAVI RDIIHRISDR FPLHILVWPV
RVQGETSGRE VAAAVKGFNV LPLEGLIPKP DLLIVARGGG SLEDLWGFND EVVVRAVYES
SLPVISAVGH ETDWTLIDYV ADWRAPTPTA AAEKAVPVKI DLEVYVVSLG ARLRTGLARY
FDFHQQKLRA IIRALPTADQ LFALPRRGFD EISSRLERAL CVSCDKKRLY FHTLAIRFTP
RLLNTEKAQH SAKEYTARLH RAFVHIVEKQ RAQLEIAFRL LKSTSYQNIL ERGFVLALGQ
NNKPIKRLAQ IPEKEQINLR FFDGEISVIT QESFFNRSSK SKRIKSKQDD QGTLF
