ID Q1DBU8_MYXXD Unreviewed; 478 AA.
AC Q1DBU8;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Peptidase, M16 (Pitrilysin) family {ECO:0000313|EMBL:ABF91009.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:ABF91009.1};
GN OrderedLocusNames=MXAN_1623 {ECO:0000313|EMBL:ABF91009.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF91009.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF91009.1, 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 M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; CP000113; ABF91009.1; -; Genomic_DNA.
DR RefSeq; WP_011551734.1; NC_008095.1.
DR AlphaFoldDB; Q1DBU8; -.
DR STRING; 246197.MXAN_1623; -.
DR EnsemblBacteria; ABF91009; ABF91009; MXAN_1623.
DR GeneID; 41359068; -.
DR KEGG; mxa:MXAN_1623; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_1_1_7; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABF91009.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 59..177
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 216..396
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 260..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 478 AA; 53184 MW; 71C8FB1079B4DE1F CRC64;
MRKVFGAVAL AAFTGCATTQ EAQKPETPPA VEAAKVEAPA EQPKLQVPVD YYKLDNGLKV
VLSRDSSAPK AVVAVYYNIG FRIEPKDRTG FAHLFEHMMF QGSTNLGKME FIRLIQKNGG
VLNGSTRFDF TNYFEVIPSN ALEPILWAEA DRMRGLDVTE ENLKNQQGVV TNEVKVNVLN
QPYGGFPWLD MPQVANTNWY NAHNFYGDLK DLEAASLEDV RAFFKTYYAP SNAALVIVGD
FEPEQVKGWI QKYFGPLPTV AQPSKPDISE PRQTKEKRHD KQDKLAQRPA LAVGYHMPDV
GTPEYFAMAL VDEVLLQGND SALYQQLVQK KGLTGEVSGG VNQLGNHWNY NGPMQWTAYL
FHDADTTTET LLAEIDGVVA QLQNQPIDAA TLERARVKAR SGLYGQLEGF LGFGRADLLA
SFALFFDDPA RINRLETELM KVTPELIQKT AKEYLRRENR TVLTVTPATA PATKTQAP
//
