XERD_BACSU
ID XERD_BACSU Reviewed; 296 AA.
AC P46352;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Tyrosine recombinase XerD;
GN Name=xerD; Synonyms=ripX, ykqM; OrderedLocusNames=BSU23510;
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=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
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 SEQUENCE REVISION TO 255.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 133-296.
RC STRAIN=168 / BR151;
RX PubMed=10537218; DOI=10.1099/00221287-145-10-2957;
RA Schuch R., Garibian A., Saxild H.H., Piggot P.J., Nygaard P.;
RT "Nucleosides as a carbon source in Bacillus subtilis: characterization of
RT the drm-pupG operon.";
RL Microbiology 145:2957-2966(1999).
RN [5]
RP FUNCTION, AND ENZYME 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:0000269|PubMed:10498718}.
CC -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two
CC molecules of XerC and two molecules of XerD. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XerD subfamily.
CC {ECO:0000305}.
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DR EMBL; D84432; BAA12649.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14283.2; -; Genomic_DNA.
DR EMBL; U32685; AAA74432.1; -; Genomic_DNA.
DR PIR; A69693; A69693.
DR RefSeq; NP_390232.2; NC_000964.3.
DR RefSeq; WP_004398985.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P46352; -.
DR SMR; P46352; -.
DR STRING; 224308.BSU23510; -.
DR PaxDb; P46352; -.
DR PRIDE; P46352; -.
DR EnsemblBacteria; CAB14283; CAB14283; BSU_23510.
DR GeneID; 938726; -.
DR KEGG; bsu:BSU23510; -.
DR PATRIC; fig|224308.179.peg.2561; -.
DR eggNOG; COG4974; Bacteria.
DR InParanoid; P46352; -.
DR OMA; HSFASHM; -.
DR PhylomeDB; P46352; -.
DR BioCyc; BSUB:BSU23510-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 HAMAP; MF_01807; Recomb_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; IPR011932; Recomb_XerD.
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; TIGR02225; recomb_XerD; 1.
DR PROSITE; PS51900; CB; 1.
DR PROSITE; PS51898; TYR_RECOMBINASE; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW DNA integration; DNA recombination; DNA-binding; Reference proteome.
FT CHAIN 1..296
FT /note="Tyrosine recombinase XerD"
FT /id="PRO_0000095371"
FT DOMAIN 1..86
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 107..290
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 147
FT /evidence="ECO:0000250"
FT ACT_SITE 171
FT /evidence="ECO:0000250"
FT ACT_SITE 242
FT /evidence="ECO:0000250"
FT ACT_SITE 245
FT /evidence="ECO:0000250"
FT ACT_SITE 268
FT /evidence="ECO:0000250"
FT ACT_SITE 277
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
FT CONFLICT 215..235
FT /note="KQISRQGFWKNLKKIALEAGI -> NRSAARILEEPEKNRIGSRH (in
FT Ref. 4; AAA74432)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="N -> D (in Ref. 1; BAA12649)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 33994 MW; 0541E31F3ECC378E CRC64;
MKDQIKDFIH YVMVERGLSQ NTIVSYERDL KSYSLYLTET LHVTDWNHVT RIHIIQYLKH
LKDSGKSGKT SARHLASIRS FHQFLLREKV TDKDPSVHIE TQKTERALPK VLALNEVERL
LDTPKLTSPF GYRDKAMLEL LYATGIRVSE MIELKTADVH LSMGFIRCFG KGRKERIVPI
GEAAASAIEE YMTKARGKLL KNNVSDALFL NHHGKQISRQ GFWKNLKKIA LEAGIKKELT
PHTLRHSFAT HLLENGADLR AVQEMLGHAD ISTTQIYTHV TKTRLKDVYK QFHPRA
