RTP_BACSU
ID RTP_BACSU Reviewed; 122 AA.
AC P0CI76; P14382; P68732;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Replication termination protein;
DE AltName: Full=Replication terminator protein;
GN Name=rtp; OrderedLocusNames=BSU18490;
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;
RX PubMed=3118336; DOI=10.1093/nar/15.20.8501;
RA Carrigan C.M., Haarsma J.A., Smith M.T., Wake R.G.;
RT "Sequence features of the replication terminus of the Bacillus subtilis
RT chromosome.";
RL Nucleic Acids Res. 15:8501-8509(1987).
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 DOMAINS, AND MUTAGENESIS.
RX PubMed=8670817; DOI=10.1002/j.1460-2075.1996.tb00679.x;
RA Pai K.S., Bussiere D.E., Wang F., Hutchison C.A. III, White S.W.,
RA Bastia D.;
RT "The structure and function of the replication terminator protein of
RT Bacillus subtilis: identification of the 'winged helix' DNA-binding
RT domain.";
RL EMBO J. 15:3164-3173(1996).
CC -!- FUNCTION: Plays a role in DNA replication and termination (fork arrest
CC mechanism). Two dimers of rtp bind to the two inverted repeat regions
CC (IRI and IRII) present in the termination site. The binding of each
CC dimer is centered on an 8 bp direct repeat.
CC -!- SUBUNIT: Homodimer.
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DR EMBL; X06168; CAA29534.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13742.1; -; Genomic_DNA.
DR PIR; A32807; A32807.
DR RefSeq; NP_389731.1; NC_000964.3.
DR RefSeq; WP_003220337.1; NZ_JNCM01000036.1.
DR PDB; 1BM9; X-ray; 2.00 A; A/B=1-122.
DR PDB; 1F4K; X-ray; 2.50 A; A/B=1-122.
DR PDB; 1J0R; X-ray; 2.50 A; A/B=1-122.
DR PDB; 2DPD; X-ray; 3.17 A; A/B=1-122.
DR PDB; 2DPU; X-ray; 3.10 A; A=1-122.
DR PDB; 2DQR; X-ray; 3.01 A; A/B/C/D=1-122.
DR PDB; 2EFW; X-ray; 2.50 A; A/B/F/G=1-122.
DR PDBsum; 1BM9; -.
DR PDBsum; 1F4K; -.
DR PDBsum; 1J0R; -.
DR PDBsum; 2DPD; -.
DR PDBsum; 2DPU; -.
DR PDBsum; 2DQR; -.
DR PDBsum; 2EFW; -.
DR AlphaFoldDB; P0CI76; -.
DR BMRB; P0CI76; -.
DR SMR; P0CI76; -.
DR STRING; 224308.BSU18490; -.
DR PaxDb; P0CI76; -.
DR PRIDE; P0CI76; -.
DR EnsemblBacteria; CAB13742; CAB13742; BSU_18490.
DR GeneID; 64303795; -.
DR GeneID; 940068; -.
DR KEGG; bsu:BSU18490; -.
DR PATRIC; fig|224308.179.peg.2016; -.
DR eggNOG; COG1695; Bacteria.
DR OMA; YGYQMLE; -.
DR EvolutionaryTrace; P0CI76; -.
DR PRO; PR:P0CI76; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006274; P:DNA replication termination; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR003432; RTP.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF02334; RTP; 1.
DR PIRSF; PIRSF021424; RTP; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome.
FT CHAIN 1..122
FT /note="Replication termination protein"
FT /id="PRO_0000097523"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:1BM9"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:1BM9"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:1J0R"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:1BM9"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:1BM9"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:1BM9"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:1BM9"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1J0R"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:1BM9"
FT HELIX 93..121
FT /evidence="ECO:0007829|PDB:1BM9"
SQ SEQUENCE 122 AA; 14519 MW; 77FC751B4BC528EA CRC64;
MKEEKRSSTG FLVKQRAFLK LYMITMTEQE RLYGLKLLEV LRSEFKEIGF KPNHTEVYRS
LHELLDDGIL KQIKVKKEGA KLQEVVLYQF KDYEAAKLYK KQLKVELDRC KKLIEKALSD
NF
