FZLC_CAUVN
ID FZLC_CAUVN Reviewed; 576 AA.
AC A0A0H3C3S1;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=FtsZ-localized protein C {ECO:0000303|PubMed:20864042};
DE AltName: Full=FtsZ-binding protein FzlC {ECO:0000305};
GN Name=fzlC {ECO:0000303|PubMed:20864042};
GN OrderedLocusNames=CCNA_00099 {ECO:0000312|EMBL:ACL93566.1};
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
RN [2]
RP INTERACTION WITH FTSZ, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=NA1000 / CB15N;
RX PubMed=20864042; DOI=10.1016/j.molcel.2010.08.027;
RA Goley E.D., Dye N.A., Werner J.N., Gitai Z., Shapiro L.;
RT "Imaging-based identification of a critical regulator of FtsZ protofilament
RT curvature in Caulobacter.";
RL Mol. Cell 39:975-987(2010).
RN [3]
RP FUNCTION, INTERACTION WITH FTSZ, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=NA1000 / CB15N;
RX PubMed=27028265; DOI=10.1111/mmi.13388;
RA Meier E.L., Razavi S., Inoue T., Goley E.D.;
RT "A novel membrane anchor for FtsZ is linked to cell wall hydrolysis in
RT Caulobacter crescentus.";
RL Mol. Microbiol. 101:265-280(2016).
CC -!- FUNCTION: Membrane anchor for FtsZ. Binds and recruits FtsZ polymers to
CC membranes early in the cell cycle. May also improve the efficiency of
CC cytokinesis through the regulation of cell wall hydrolysis.
CC {ECO:0000269|PubMed:27028265}.
CC -!- SUBUNIT: Interacts with FtsZ filaments. {ECO:0000269|PubMed:20864042,
CC ECO:0000269|PubMed:27028265}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27028265}. Cell
CC inner membrane {ECO:0000269|PubMed:27028265}. Note=Associates with
CC membranes directly (PubMed:27028265). Colocalizes with FtsZ at the
CC division site (PubMed:20864042). {ECO:0000269|PubMed:20864042,
CC ECO:0000269|PubMed:27028265}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant grows with normal rates,
CC morphology and Z-ring organization (PubMed:20864042, PubMed:27028265).
CC In cells lacking other non-essential division genes implicated in cell
CC wall hydrolysis, such as dipM, ftsE or amiC, deletion of fzlC causes
CC synthetic cytokinesis defects (PubMed:27028265).
CC {ECO:0000269|PubMed:20864042, ECO:0000269|PubMed:27028265}.
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DR EMBL; CP001340; ACL93566.1; -; Genomic_DNA.
DR RefSeq; WP_010917989.1; NC_011916.1.
DR RefSeq; YP_002515474.1; NC_011916.1.
DR AlphaFoldDB; A0A0H3C3S1; -.
DR SMR; A0A0H3C3S1; -.
DR EnsemblBacteria; ACL93566; ACL93566; CCNA_00099.
DR GeneID; 7332353; -.
DR KEGG; ccs:CCNA_00099; -.
DR PATRIC; fig|565050.3.peg.98; -.
DR HOGENOM; CLU_025266_0_0_5; -.
DR OMA; IDRMMPM; -.
DR OrthoDB; 442785at2; -.
DR PhylomeDB; A0A0H3C3S1; -.
DR Proteomes; UP000001364; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR Gene3D; 1.50.10.100; -; 1.
DR InterPro; IPR008929; Chondroitin_lyas.
DR InterPro; IPR012480; Hepar_II_III.
DR Pfam; PF07940; Hepar_II_III; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; Cytoplasm;
KW Membrane; Reference proteome.
FT CHAIN 1..576
FT /note="FtsZ-localized protein C"
FT /id="PRO_0000444997"
SQ SEQUENCE 576 AA; 61333 MW; 4FFD491EEB23F015 CRC64;
MAGKPPVLGL AFPARLRGGV LWKAIRAEAA GHVEREWFGS GPHRLKIALP RPEGLSARPH
DPRPVDPAHG QKILSGALTL DGGALRLGVD GDPFDTASPS RRFAVSLHRF DWLPDLVAVG
PDGARRALRL IDDWRRVFGK WNAFSWGPEC LERRVHHLAC AAKTLAAEAS DAEVADLVFD
LARQGRHLLE ITRAPERTLE RAVAAGLAGC VLAGKPGEPL IDAALKALVP QLDAMVLGDG
GHATRSPEAG VELLFDLLTL DDALGQRGRP SPEALSRAID RLSSATRFFI LGDGHLAAFH
GGETVGPARI AAALAHDDAG PRSLNAAPHS GYHKMIGGSI EVIADCGPPP VGPLSVNACA
QPAAFEIVCA KDRLITSCGW SPEAAGAHAF RLSDAASTVS VADGSAGRPL SGFRAKALGP
WLVDGAAKVE AKRHDDVGGV WLDIVHDGWR HLGLTHARRL FLDAVQDELR GEDSLSPLAL
DPKAAEGPRR YLPFAVRFHL HPDARASIAR DGKSVLIRGP SNIGWWLRND AVDVEIAPSA
HFDHGLARKA GQIVLKSQVR PEVGAKIRWK LTKAEG