ID B9E6Q8_MACCJ Unreviewed; 445 AA.
AC B9E6Q8;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
DE EC=3.1.11.6 {ECO:0000256|HAMAP-Rule:MF_00378};
DE AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
DE Short=Exonuclease VII large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
GN Name=xseA {ECO:0000256|HAMAP-Rule:MF_00378};
GN OrderedLocusNames=MCCL_1169 {ECO:0000313|EMBL:BAH17876.1};
OS Macrococcus caseolyticus (strain JCSC5402).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX NCBI_TaxID=458233 {ECO:0000313|EMBL:BAH17876.1, ECO:0000313|Proteomes:UP000001383};
RN [1] {ECO:0000313|EMBL:BAH17876.1, ECO:0000313|Proteomes:UP000001383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC5402 {ECO:0000313|EMBL:BAH17876.1,
RC ECO:0000313|Proteomes:UP000001383};
RX PubMed=19074389; DOI=10.1128/JB.01058-08;
RA Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL J. Bacteriol. 191:1180-1190(2009).
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:0000256|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:0000256|HAMAP-Rule:MF_00378,
CC ECO:0000256|RuleBase:RU004355};
CC -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00378}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00378,
CC ECO:0000256|RuleBase:RU004355}.
CC -!- SIMILARITY: Belongs to the XseA family. {ECO:0000256|HAMAP-
CC Rule:MF_00378, ECO:0000256|RuleBase:RU004355}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP009484; BAH17876.1; -; Genomic_DNA.
DR AlphaFoldDB; B9E6Q8; -.
DR STRING; 458233.MCCL_1169; -.
DR KEGG; mcl:MCCL_1169; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_9; -.
DR Proteomes; UP000001383; 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00378};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_00378};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00378};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00378};
KW Reference proteome {ECO:0000313|Proteomes:UP000001383}.
FT DOMAIN 8..103
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 126..439
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
SQ SEQUENCE 445 AA; 50719 MW; A4F92E48DB605CA6 CRC64;
MIIMEKYLSV SALTRYIKTK FDKDPYLTEV YIKGELSNFK RHSSGHLYFA LKDNDGVISC
MMFKRDAAQL TFSPKEGDSV LITGRVSVYE GRGNYQLYAT DIRLDGIGVL YERLEALKKK
YFEKGYFNVE NKKQLPKYPE HIAVLTASTG AAVQDIRTTL SSRYPLAEVT YISTIVQGEA
AKDDIVNNLN TADQLGADVI IVGRGGGSIE DLWAFNEEGV VEAIYACNTP VISAVGHETD
TTLSDLVADH RAPTPTAAAV MATPDSRELL VGLKQVDITM LRTMNQRIKR NNERLNYLSS
YYIFKNPYML IEQKMQKLDD FEHRMKLASF SLINQNKMNF HFISNKIDAQ KLNTKLKYQY
EQIHSMQNVM KRTLSYKLSN YHQQLKHQIA LLSSLSPAET LLRGYAIVRS EDEIIKSVYD
VKEHDYVNIQ LNDGRIKAEV KHINK
//