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Counting factor 50 (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase 1) (GH family 25 lysozyme 1)

 CF50_DICDI              Reviewed;         303 AA.
Q556R7; Q86JX6; Q95VT3;
29-APR-2008, integrated into UniProtKB/Swiss-Prot.
02-MAY-2006, sequence version 1.
28-MAR-2018, entry version 80.
RecName: Full=Counting factor 50;
EC=3.2.1.17;
AltName: Full=1,4-beta-N-acetylmuramidase 1;
AltName: Full=GH family 25 lysozyme 1;
Flags: Precursor;
Name=cf50-1; ORFNames=DDB_G0273175;
and
Name=cf50-2; ORFNames=DDB_G0273875;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
Dictyosteliaceae; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-42,
IDENTIFICATION IN THE CF COMPLEX, SUBUNIT, AND DISRUPTION PHENOTYPE.
PubMed=12117815;
Brock D.A., Hatton R.D., Giurgiutiu D.-V., Scott B., Ammann R.,
Gomer R.H.;
"The different components of a multisubunit cell number-counting
factor have both unique and overlapping functions.";
Development 129:3657-3668(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=12097910; DOI=10.1038/nature00847;
Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A.,
Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G.,
Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A.,
Platzer M., Rosenthal A., Noegel A.A.;
"Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
Nature 418:79-85(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[4]
IDENTIFICATION IN THE CF COMPLEX.
PubMed=10444594; DOI=10.1101/gad.13.15.1960;
Brock D.A., Gomer R.H.;
"A cell-counting factor regulating structure size in Dictyostelium.";
Genes Dev. 13:1960-1969(1999).
[5]
IDENTIFICATION IN THE CF COMPLEX.
PubMed=12912898; DOI=10.1128/EC.2.4.788-797.2003;
Brock D.A., Hatton R.D., Giurgiutiu D.-V., Scott B., Jang W.,
Ammann R., Gomer R.H.;
"CF45-1, a secreted protein which participates in Dictyostelium group
size regulation.";
Eukaryot. Cell 2:788-797(2003).
[6]
IDENTIFICATION IN THE CF COMPLEX.
PubMed=16963635; DOI=10.1128/EC.00169-06;
Brock D.A., van Egmond W.N., Shamoo Y., Hatton R.D., Gomer R.H.;
"A 60-kilodalton protein component of the counting factor complex
regulates group size in Dictyostelium discoideum.";
Eukaryot. Cell 5:1532-1538(2006).
-!- FUNCTION: Cell-counting factor that limits the maximum size of the
multicellular structure during aggregation. Has a very low
lysozyme activity.
-!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-linkages between N-
acetylmuramic acid and N-acetyl-D-glucosamine residues in a
peptidoglycan and between N-acetyl-D-glucosamine residues in
chitodextrins.
-!- SUBUNIT: Monomer. Component of the counting factor (CF) complex,
which includes cf60, cf50, cf45-1 and ctnA.
{ECO:0000269|PubMed:10444594, ECO:0000269|PubMed:12117815,
ECO:0000269|PubMed:12912898, ECO:0000269|PubMed:16963635}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- DISRUPTION PHENOTYPE: In the absence of CF50, secreted countin is
degraded suggesting that it may protect countin from degradation.
{ECO:0000269|PubMed:12117815}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family.
{ECO:0000305}.
-!- CAUTION: The gene for this protein is duplicated in strains AX3
and AX4. These strains contain a duplication of a segment of 750
kb of chromosome 2 compared to the corresponding sequence in
strain AX2. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF405695; AAL01036.1; -; Genomic_DNA.
EMBL; AAFI02000011; EAL70628.1; -; Genomic_DNA.
EMBL; AAFI02000009; EAL70805.1; -; Genomic_DNA.
RefSeq; XP_644554.1; XM_639462.1.
RefSeq; XP_644697.1; XM_639605.1.
ProteinModelPortal; Q556R7; -.
SMR; Q556R7; -.
STRING; 44689.DDB0266487; -.
PaxDb; Q556R7; -.
EnsemblProtists; EAL70628; EAL70628; DDB_G0273875.
EnsemblProtists; EAL70805; EAL70805; DDB_G0273175.
GeneID; 8618796; -.
GeneID; 8619180; -.
KEGG; ddi:DDB_G0273175; -.
KEGG; ddi:DDB_G0273875; -.
dictyBase; DDB_G0273175; cf50-1.
dictyBase; DDB_G0273875; cf50-2.
eggNOG; ENOG410IZBF; Eukaryota.
eggNOG; ENOG41124VU; LUCA.
InParanoid; Q556R7; -.
OMA; VIDPDYN; -.
PhylomeDB; Q556R7; -.
PRO; PR:Q556R7; -.
Proteomes; UP000002195; Chromosome 2.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0005576; C:extracellular region; IDA:dictyBase.
GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
GO; GO:0004871; F:signal transducer activity; IMP:dictyBase.
GO; GO:0030154; P:cell differentiation; IMP:dictyBase.
GO; GO:0048870; P:cell motility; IMP:dictyBase.
GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
GO; GO:0098609; P:cell-cell adhesion; IMP:dictyBase.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
GO; GO:0042593; P:glucose homeostasis; IMP:dictyBase.
GO; GO:0031158; P:negative regulation of aggregate size involved in sorocarp development; IMP:dictyBase.
GO; GO:0045861; P:negative regulation of proteolysis; IMP:dictyBase.
GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
InterPro; IPR002053; Glyco_hydro_25.
InterPro; IPR017853; Glycoside_hydrolase_SF.
Pfam; PF01183; Glyco_hydro_25; 1.
SUPFAM; SSF51445; SSF51445; 1.
1: Evidence at protein level;
Antimicrobial; Bacteriolytic enzyme; Complete proteome;
Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 24 {ECO:0000269|PubMed:12117815}.
CHAIN 25 303 Counting factor 50.
/FTId=PRO_0000330647.
REGION 226 303 S-G-S motif repeats.
COMPBIAS 227 302 Ser-rich.
ACT_SITE 125 125 {ECO:0000250}.
CARBOHYD 67 67 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 170 170 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 303 AA; 30854 MW; 2B2A3CC1CEE3CE8A CRC64;
MNKMNNIFLI ISSIILSIVI FVSGECAIDF SSEISVGISD SQWSCLASNN QRVIIQVWSG
GGQYNSNISS VVSAAEQAGF DNIDLYAFLC SECDGNYPAS SAIQSLVSSL KSDGINFNML
WIDVEQCDGC WGAESDNADY VQEAVETAQG LGVLVGVYSS EGEWPQTVGN LSTLSQYPLW
YAHYDDNPSF SDTAFYEFGG WTSPAMKQYI GNTNQCGVSV DLDFYGSGSG CSTSSGSASG
SASGSASGSA SGSNSGSSNS GSSNSGSSNS GSNSGSSNSG SGNSGSSNSG SASGSGTGSG
SSI


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