XERC_BACSU
ID XERC_BACSU Reviewed; 304 AA.
AC P39776;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; Synonyms=codV;
GN OrderedLocusNames=BSU16140;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=7783641; DOI=10.1111/j.1365-2958.1995.tb02378.x;
RA Slack F.J., Serror P., Joyce E., Sonenshein A.L.;
RT "A gene required for nutritional repression of the Bacillus subtilis
RT dipeptide permease operon.";
RL Mol. Microbiol. 15:689-702(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-85.
RC STRAIN=168;
RA Foulger D., Errington J.;
RT "Cloning and sequencing 7.5 Kbp of DNA from Bacillus subtilis upstream of
RT the codV gene.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP DNA-BINDING ACTIVITY.
RX PubMed=10498718; DOI=10.1128/jb.181.19.6053-6062.1999;
RA Sciochetti S.A., Piggot P.J., Sherratt D.J., Blakely G.;
RT "The ripX locus of Bacillus subtilis encodes a site-specific recombinase
RT involved in proper chromosome partitioning.";
RL J. Bacteriol. 181:6053-6062(1999).
CC -!- FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing
CC the cutting and rejoining of the recombining DNA molecules. The XerC-
CC XerD complex is essential to convert dimers of the bacterial chromosome
CC into monomers to permit their segregation at cell division. It also
CC contributes to the segregational stability of plasmids.
CC {ECO:0000255|HAMAP-Rule:MF_01808}.
CC -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two
CC molecules of XerC and two molecules of XerD. {ECO:0000255|HAMAP-
CC Rule:MF_01808}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01808}.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XerC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01808}.
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DR EMBL; U13634; AAB03369.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13487.1; -; Genomic_DNA.
DR EMBL; AJ000975; CAA04424.1; -; Genomic_DNA.
DR PIR; G69601; G69601.
DR RefSeq; NP_389496.1; NC_000964.3.
DR RefSeq; WP_003231988.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P39776; -.
DR SMR; P39776; -.
DR STRING; 224308.BSU16140; -.
DR PaxDb; P39776; -.
DR PRIDE; P39776; -.
DR EnsemblBacteria; CAB13487; CAB13487; BSU_16140.
DR GeneID; 938003; -.
DR KEGG; bsu:BSU16140; -.
DR PATRIC; fig|224308.179.peg.1754; -.
DR eggNOG; COG4974; Bacteria.
DR InParanoid; P39776; -.
DR OMA; QAFWYLI; -.
DR PhylomeDB; P39776; -.
DR BioCyc; BSUB:BSU16140-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009037; F:tyrosine-based site-specific recombinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.150.130; -; 1.
DR Gene3D; 1.10.443.10; -; 1.
DR HAMAP; MF_01808; Recomb_XerC_XerD; 1.
DR InterPro; IPR044068; CB.
DR InterPro; IPR011010; DNA_brk_join_enz.
DR InterPro; IPR013762; Integrase-like_cat_sf.
DR InterPro; IPR002104; Integrase_catalytic.
DR InterPro; IPR010998; Integrase_recombinase_N.
DR InterPro; IPR004107; Integrase_SAM-like_N.
DR InterPro; IPR011931; Recomb_XerC.
DR InterPro; IPR023009; Tyrosine_recombinase_XerC/XerD.
DR Pfam; PF02899; Phage_int_SAM_1; 1.
DR Pfam; PF00589; Phage_integrase; 1.
DR SUPFAM; SSF56349; SSF56349; 1.
DR TIGRFAMs; TIGR02224; recomb_XerC; 1.
DR PROSITE; PS51900; CB; 1.
DR PROSITE; PS51898; TYR_RECOMBINASE; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW DNA integration; DNA recombination; DNA-binding; Reference proteome.
FT CHAIN 1..304
FT /note="Tyrosine recombinase XerC"
FT /id="PRO_0000095284"
FT DOMAIN 2..88
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 109..294
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 149
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 173
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 246
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 249
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 272
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 281
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
SQ SEQUENCE 304 AA; 35342 MW; B0778DBDA065A053 CRC64;
MENVKNFVKL FVEYLQIEKN YSQYTIVNYV DSIEEFETFL RVQGINGFEE AAYQDTRIFL
TEAYEKGLSR RTISKKISAL RSFYKFLMRE KLIEENPFQL VHLPKQEKRI PKFLYQKELE
ELFEVSDISQ PAGMRDQALL ELLYATGMRV SECCSITIND VDLFMDTVLV HGKGKKQRYI
PFGSYAREAL KVYMNSGRQC LLMKAKEPHD LLFVNQRGGP LTARGIRHIL SGLVQKASST
LHIHPHMLRH TFATHLLNEG ADLRSVQELL GHSNLSSTQI YTHVSKEMLR NTYMSHHPRA
FKKN
