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CRFC_ECOLI
ID   CRFC_ECOLI              Reviewed;         742 AA.
AC   P0DM85; P16694; Q2M6J5;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   11-DEC-2013, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Clamp-binding protein CrfC;
DE   AltName: Full=Clamp-binding sister replication fork colocalization protein;
GN   Name=crfC; Synonyms=yjdA; OrderedLocusNames=b4109, JW4070;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT   from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION, LACK OF GTPASE, INTERACTION WITH DNAN, SUBUNIT, SUBCELLULAR
RP   LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLN-23; GLN-41 AND
RP   GLN-734.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=23994470; DOI=10.1016/j.celrep.2013.07.040;
RA   Ozaki S., Matsuda Y., Keyamura K., Kawakami H., Noguchi Y., Kasho K.,
RA   Nagata K., Masuda T., Sakiyama Y., Katayama T.;
RT   "A replicase clamp-binding dynamin-like protein promotes colocalization of
RT   nascent DNA strands and equipartitioning of chromosomes in E. coli.";
RL   Cell Rep. 4:985-995(2013).
CC   -!- FUNCTION: Important for the colocalization of sister nascent DNA
CC       strands after replication fork passage during DNA replication, and for
CC       positioning and subsequent partitioning of sister chromosomes. Does not
CC       have GTPase activity on its own. {ECO:0000269|PubMed:23994470}.
CC   -!- SUBUNIT: Forms homooligomers. Binds to the beta sliding clamp
CC       processivity factor (DnaN) in the presence and absence of DNA, may bind
CC       to the clamp itself as homodimers or trimers. Homooligomers may be able
CC       to bind more than 1 clamp complex. {ECO:0000269|PubMed:23994470}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23994470}.
CC       Note=About half the protein co-localizes with beta sliding clamp (DnaN)
CC       at midcell, the rest without clamp in quarter-cell positions when
CC       chromosomes are condensed during DNA replication.
CC   -!- DISRUPTION PHENOTYPE: A small proportion of anucleate cells, disrupts
CC       nucleoid positioning, leads to premature separation of sister
CC       replication forks. {ECO:0000269|PubMed:23994470}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01055}.
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DR   EMBL; U14003; AAA97008.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77070.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78111.1; -; Genomic_DNA.
DR   PIR; S56337; S56337.
DR   RefSeq; NP_418533.1; NC_000913.3.
DR   RefSeq; WP_000288603.1; NZ_LN832404.1.
DR   AlphaFoldDB; P0DM85; -.
DR   BioGRID; 4263087; 6.
DR   BioGRID; 852912; 2.
DR   IntAct; P0DM85; 13.
DR   STRING; 511145.b4109; -.
DR   PaxDb; P0DM85; -.
DR   PRIDE; P0DM85; -.
DR   EnsemblBacteria; AAC77070; AAC77070; b4109.
DR   EnsemblBacteria; BAE78111; BAE78111; BAE78111.
DR   GeneID; 948620; -.
DR   KEGG; ecj:JW4070; -.
DR   KEGG; eco:b4109; -.
DR   PATRIC; fig|511145.12.peg.4240; -.
DR   EchoBASE; EB1195; -.
DR   eggNOG; COG0699; Bacteria.
DR   HOGENOM; CLU_011600_2_0_6; -.
DR   OMA; QRWVQDF; -.
DR   BioCyc; EcoCyc:EG11210-MON; -.
DR   PRO; PR:P0DM85; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0043590; C:bacterial nucleoid; IDA:EcoCyc.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; IDA:EcoCyc.
DR   GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR   GO; GO:0007059; P:chromosome segregation; IMP:EcoCyc.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:1900231; P:regulation of single-species biofilm formation on inanimate substrate; IMP:EcoCyc.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR045063; Dynamin_N.
DR   InterPro; IPR030381; G_DYNAMIN_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51718; G_DYNAMIN_2; 1.
PE   1: Evidence at protein level;
KW   Chromosome partition; Coiled coil; Cytoplasm; DNA replication;
KW   Reference proteome.
FT   CHAIN           1..742
FT                   /note="Clamp-binding protein CrfC"
FT                   /id="PRO_0000169728"
FT   DOMAIN          66..402
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          41..45
FT                   /note="Clamp-binding consensus"
FT   REGION          76..83
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          102..104
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          236..239
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          297..300
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          331..334
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   COILED          440..472
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         23
FT                   /note="Q->A: Interacts with beta sliding clamp."
FT                   /evidence="ECO:0000269|PubMed:23994470"
FT   MUTAGEN         41
FT                   /note="Q->A: No longer interacts with beta sliding clamp,
FT                   pattern of CrfC foci changes."
FT                   /evidence="ECO:0000269|PubMed:23994470"
FT   MUTAGEN         734
FT                   /note="Q->A: Interacts with beta sliding clamp."
FT                   /evidence="ECO:0000269|PubMed:23994470"
SQ   SEQUENCE   742 AA;  84371 MW;  8A7008FC16A026B3 CRC64;
     MYTQTLYELS QEAERLLQLS RQQLQLLEKM PLSVPGDDAP QLALPWSQPN IAERHAMLNN
     ELRKISRLEM VLAIVGTMKA GKSTTINAIV GTEVLPNRNR PMTALPTLIR HTPGQKEPVL
     HFSHVAPIDC LIQQLQQRLR DCDIKHLTDV LEIDKDMRAL MQRIENGVAF EKYYLGAQPI
     FHCLKSLNDL VRLAKALDVD FPFSAYAAIE HIPVIEVEFV HLAGLESYPG QLTLLDTPGP
     NEAGQPHLQK MLNQQLARAS AVLAVLDYTQ LKSISDEEVR EAILAVGQSV PLYVLVNKFD
     QQDRNSDDAD QVRALISGTL MKGCITPQQI FPVSSMWGYL ANRARYELAN NGKLPPPEQQ
     RWVEDFAHAA LGRRWRHADL ADLEHIRHAA DQLWEDSLFA QPIQALLHAA YANASLYALR
     SAAHKLLNYA QQAREYLDFR AHGLNVACEQ LRQNIHQIEE SLQLLQLNQA QVSGEIKHEI
     ELALTSANHF LRQQQDALKV QLAALFQDDS EPLSEIRTRC ETLLQTAQNT ISRDFTLRFA
     ELESTLCRVL TDVIRPIEQQ VKMELSESGF RPGFHFPVFH GVVPHFNTRQ LFSEVISRQE
     ATDEQSTRLG VVRETFSRWL NQPDWGRGNE KSPTETVDYS VLQRALSAEV DLYCQQMAKV
     LAEQVDESVT AGMNTFFAEF ASCLTELQTR LRESLALRQQ NESVVRLMQQ QLQQTVMTHG
     WIYTDAQLLR DDIQTLFTAE RY
 
 
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