ID   FRZCD_MYXXA             Reviewed;         417 AA.
AC   P43500;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Frizzy aggregation protein FrzCD;
GN   Name=frzCD;
OS   Myxococcus xanthus.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=34;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2492105; DOI=10.1073/pnas.86.2.424;
RA   McBride M.J., Weinberg R.A., Zusman D.R.;
RT   "'Frizzy' aggregation genes of the gliding bacterium Myxococcus xanthus
RT   show sequence similarities to the chemotaxis genes of enteric bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:424-428(1989).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=1624419; DOI=10.1128/jb.174.13.4246-4257.1992;
RA   McBride M.J., Kohler T., Zusman D.R.;
RT   "Methylation of FrzCD, a methyl-accepting taxis protein of Myxococcus
RT   xanthus, is correlated with factors affecting cell behavior.";
RL   J. Bacteriol. 174:4246-4257(1992).
CC   -!- FUNCTION: Methyl-accepting taxis protein necessary for the proper
CC       aggregation of cells to form fruiting bodies. Frz genes define a system
CC       of signal transduction analogous to the enterobacterial chemotaxis
CC       systems.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: Methylated. Saturated fatty acids capric acid and lauric acid
CC       stimulate methylation. Short-chain alcohols, such as isoamyl alcohol,
CC       and some other solvents cause demethylation.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; J04157; AAA25395.1; -; Genomic_DNA.
DR   PIR; C32185; C32185.
DR   RefSeq; WP_011554144.1; NZ_FNOH01000003.1.
DR   AlphaFoldDB; P43500; -.
DR   SMR; P43500; -.
DR   GeneID; 41361460; -.
DR   OMA; KHASAQI; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   Pfam; PF00015; MCPsignal; 1.
DR   SMART; SM00283; MA; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE   1: Evidence at protein level;
KW   Chemotaxis; Cytoplasm; Methylation; Transducer.
FT   CHAIN           1..417
FT                   /note="Frizzy aggregation protein FrzCD"
FT                   /id="PRO_0000110546"
FT   DOMAIN          144..380
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   417 AA;  43584 MW;  2AC3A70BB26070C7 CRC64;
     MSLDTPNEKP AGKARARKAP ASKAGATNAA STSSSTKAIT DTLLTVLSGN LQARVPKELV
     GESGVELAHL LNQVLDQFAA SEHRKHVAAQ EIDQALDALI GLVREGDLSR WNTTTEDPQL
     GPLLEGFGKV IETLRTFVRE INEAALRLSS SANQVLAAST QHETSSTEQA AAIHETTATM
     EELKHASAQI AENAGSVARV AEETLGAARA GRGAIGEFIQ AMQQIRSDGV AVADSIAKLS
     KRVERIGTVV EVIDEIADRS DLLALNAALE GSRAGEAGKG FSIVAAEMRR LAENVLDSTK
     EIKNLITEIR EATAAAAGAA EASKSATESG EKLGAVAAQA VEGILAGVQE TSDAARVINL
     ATQQQRTATE QVVASMAEIE DVTRQTTQAS KQATGAAAEL TQLAGRLAEL IKRFKAD