ID Q1DE46_MYXXD Unreviewed; 345 AA.
AC Q1DE46;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 08-OCT-2025, entry version 104.
DE RecName: Full=Serine protease {ECO:0000256|RuleBase:RU004296};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU004296};
GN OrderedLocusNames=MXAN_0814 {ECO:0000313|EMBL:ABF88667.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF88667.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF88667.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC -!- SIMILARITY: Belongs to the peptidase S1B family.
CC {ECO:0000256|ARBA:ARBA00008764, ECO:0000256|RuleBase:RU004296}.
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DR EMBL; CP000113; ABF88667.1; -; Genomic_DNA.
DR RefSeq; WP_011550937.1; NC_008095.1.
DR AlphaFoldDB; Q1DE46; -.
DR STRING; 246197.MXAN_0814; -.
DR EnsemblBacteria; ABF88667; ABF88667; MXAN_0814.
DR GeneID; 41358280; -.
DR KEGG; mxa:MXAN_0814; -.
DR eggNOG; COG3591; Bacteria.
DR HOGENOM; CLU_762498_0_0_7; -.
DR OrthoDB; 513782at2; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR045430; EAD1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR008256; Peptidase_S1B.
DR Pfam; PF19955; EAD1; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00839; V8PROTEASE.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004296};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004296};
KW Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004296}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1..86
FT /note="Effector-associated"
FT /evidence="ECO:0000259|Pfam:PF19955"
SQ SEQUENCE 345 AA; 37810 MW; FDED3A5F439ABA41 CRC64;
MELDGAERDE LQRALTSAFA SVEHLRRVVA ATCRRDLEAL GVSGGLRERV FALIHMAEAE
GWLRELIRGV YQALPRHPRL QRFVQVYLAS IQRSIPRVGL ERIFGSGRAD AEREHWRKRL
TSIERQVCRV EPEVGAALGT GFLVSPSVVL TNFHVIENRL LESLRVRFGR KVLQDGTLLH
PGTVYRVTRC LARSPYSPAD LMHPRPRDAT SGELDYAFLE VAGVPGEDLV DGEPRGWLEP
PDSRESFTPG SLVLIVQHPA GQPMSVALDE FLGVNPGRTR VAYRACTGPG SSGAPCFTQD
LRLAALHHSG GPRVPSASVG HNEGIPIDTI RGSLSGSMLS QLGWG
//
