ID   Q1D193_MYXXD            Unreviewed;       341 AA.
AC   Q1D193;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   SubName: Full=Peptidase, S1 (Chymotrypsin) family {ECO:0000313|EMBL:ABF91256.1};
DE            EC=3.4.21.4 {ECO:0000313|EMBL:ABF91256.1};
GN   OrderedLocusNames=MXAN_5435 {ECO:0000313|EMBL:ABF91256.1};
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF91256.1, ECO:0000313|Proteomes:UP000002402};
RN   [1] {ECO:0000313|EMBL:ABF91256.1, 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).
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DR   EMBL; CP000113; ABF91256.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1D193; -.
DR   STRING; 246197.MXAN_5435; -.
DR   EnsemblBacteria; ABF91256; ABF91256; MXAN_5435.
DR   KEGG; mxa:MXAN_5435; -.
DR   eggNOG; COG5640; Bacteria.
DR   HOGENOM; CLU_006842_7_3_7; -.
DR   OrthoDB; 1496095at2; -.
DR   Proteomes; UP000002402; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 3.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR   PANTHER; PTHR24252:SF7; HYALIN; 1.
DR   Pfam; PF00089; Trypsin; 2.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:ABF91256.1};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW   Serine protease {ECO:0000256|RuleBase:RU363034}.
FT   DOMAIN          55..334
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   341 AA;  36036 MW;  9333E482678592E7 CRC64;
     MRHGMWLAVG MCLMSKEGAL RFVSGVIVAV SLLGCGGPEL ERQDVEATGR MDQAIVGGVE
     ARPGSHPWIV SLQQYNDHFC GGSLIRVGNK EESDIVVTAA HCVYDGTSGL TVVAGAHDFN
     RPSSSQQAVV ARKTVYHPEY NPDTTANDVA VVVLDKPIKF TSTVQPVCLP EDSFSVSGAS
     CGKSSVVMRP NLVAKSPLAE TSLSPVGLSS VGADVPDGTM MVTAGWGLIR EGGYDTSSIL
     MQVWVPTVNS ETLKTAYKKE GITIDPNVML GAGYMSGGKD SCQGDSGGPL VAQVGGRYVL
     YGITSFGVGC ARPGFPGVYA RVSEFRSWIN TQVKDNSRSR Y
//