ID   CRFC_ECOLX              Reviewed;         742 AA.
AC   P0DM86; P16694; Q2M6J5;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   11-DEC-2013, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Clamp-binding protein CrfC;
DE   AltName: Full=Clamp-binding sister replication fork colocalization protein;
GN   Name=crfC; Synonyms=yjdA;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B;
RX   PubMed=2155230; DOI=10.1016/s0021-9258(19)39587-0;
RA   Chen C.-M., Ye Q.-Z., Zhu Z., Wanner B.L., Walsh C.T.;
RT   "Molecular biology of carbon-phosphorus bond cleavage. Cloning and
RT   sequencing of the phn (psiD) genes involved in alkylphosphonate uptake and
RT   C-P lyase activity in Escherichia coli B.";
RL   J. Biol. Chem. 265:4461-4471(1990).
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=About half the
CC       protein co-localizes with beta sliding clamp (DnaN) at midcell, the
CC       rest without clamp in quarter-cell positions when chromosomes are
CC       condensed during DNA replication. {ECO:0000250}.
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; J05260; AAA24336.1; -; Genomic_DNA.
DR   PIR; S56337; S56337.
DR   RefSeq; WP_000288588.1; NZ_WVVZ01000009.1.
DR   AlphaFoldDB; P0DM86; -.
DR   STRING; 585034.ECIAI1_4338; -.
DR   OMA; QRWVQDF; -.
DR   OrthoDB; 383368at2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Chromosome partition; Coiled coil; Cytoplasm; DNA replication.
FT   CHAIN           1..742
FT                   /note="Clamp-binding protein CrfC"
FT                   /id="PRO_0000424595"
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                   /evidence="ECO:0000250"
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"
SQ   SEQUENCE   742 AA;  84209 MW;  F204891227DE33C7 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 ANRARHELAN NGKLPAPEQQ
     RWVEDFAHAA LGRRWRHADL ADLEHIRHAA DQLWEDSLFA QPIQALLHAA YANASLYALR
     SAAHKLLNYA QQAREYLDFR AHGLNVACEQ LRQNIHQVEE SLQLLQLNQA QVSGEIKHEI
     ELALTSANHF LRQQQDALNA QLAALFQDDS EPLSEMRTRC ETLLQTAQNT ISRDFTLRFA
     ELESTLCRVL TDVIRPIEQQ VKMELSESGF RPGFHFPVFH GVVPHFNTRQ LFSAVISRQD
     ATDEQSTRLG VVRETFSRWL NQPDWGRGNE KSPTETVDYS VLQRALSAEV DLYCQQMAKV
     LAEQVDESVT AGMNTFFAEF ASCLTELQTR LRESLALRQQ NESVVRLMQQ QLQQTVMTHG
     WIYTDAQLLR DDIQTLFTAE RY