ID Q1D272_MYXXD Unreviewed; 437 AA.
AC Q1D272;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=M20 (Carboxypeptidase Ss1) subfamily protein {ECO:0000313|EMBL:ABF92271.1};
DE EC=3.4.-.- {ECO:0000313|EMBL:ABF92271.1};
GN OrderedLocusNames=MXAN_5097 {ECO:0000313|EMBL:ABF92271.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF92271.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF92271.1, 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; ABF92271.1; -; Genomic_DNA.
DR RefSeq; WP_011555071.1; NC_008095.1.
DR AlphaFoldDB; Q1D272; -.
DR STRING; 246197.MXAN_5097; -.
DR EnsemblBacteria; ABF92271; ABF92271; MXAN_5097.
DR GeneID; 41362381; -.
DR KEGG; mxa:MXAN_5097; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_6_0_7; -.
DR OrthoDB; 9777385at2; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ABF92271.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..437
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004188151"
FT DOMAIN 220..315
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 437 AA; 46073 MW; BFE49C71A7B0A261 CRC64;
MKISPLLPLL LISLAAPGGL ALAAETPPVL GGLDAIYPEL DALYRDLHQT PELSNQEAKT
AAKLADRLRK LGFEVTSKVG GHGVVALLRN GQGPTVMLRA DMDALPVEEK TGLPYASKQK
AKDAAGATHP VMHACGHDVH MTSLLGTAAL LARSKDRWRG TLLLVGQPAE EVGAGARQML
QDGLFKRFPK PDFAVALHVN TAAAGTVEFT PGYAMASVDG VEITLHGKGG HGAYPHTTVD
PVVMAARVVL SLQTLVSREK NPLEPAVVTV GSIHGGAKHN IIPDDVKLHL TVRSYKPEVR
KALLDGIERI AKAEAMASGA PRPPDIAITE GTPSTFNDPA LTKRLVGAVS RVLGEKNLQE
APPVMGGEDF SEYGRAGVPA VMLWLGSTEP RQYAQAMSAG TALPSMHSPL FAPDRERTLR
TGVTTLTTAA LELLGKP
//
