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Database: UniProt
Entry: Q1D204_MYXXD
LinkDB: Q1D204_MYXXD
Original site: Q1D204_MYXXD 
ID   Q1D204_MYXXD            Unreviewed;       402 AA.
AC   Q1D204;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   24-JAN-2024, entry version 98.
DE   SubName: Full=Bacterial leucyl aminopeptidase {ECO:0000313|EMBL:ABF89324.1};
DE            EC=3.4.11.10 {ECO:0000313|EMBL:ABF89324.1};
GN   OrderedLocusNames=MXAN_5166 {ECO:0000313|EMBL:ABF89324.1};
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF89324.1, ECO:0000313|Proteomes:UP000002402};
RN   [1] {ECO:0000313|EMBL:ABF89324.1, 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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036685-1};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR036685-
CC       1};
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DR   EMBL; CP000113; ABF89324.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1D204; -.
DR   STRING; 246197.MXAN_5166; -.
DR   EnsemblBacteria; ABF89324; ABF89324; MXAN_5166.
DR   KEGG; mxa:MXAN_5166; -.
DR   eggNOG; COG2234; Bacteria.
DR   HOGENOM; CLU_025866_2_1_7; -.
DR   OMA; GMLQQDM; -.
DR   Proteomes; UP000002402; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR012189; Pept_M28E_Ap1.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147:SF26; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1; 1.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   PIRSF; PIRSF036685; BacLeuNPeptidase; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Aminopeptidase {ECO:0000313|EMBL:ABF89324.1};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR036685-2};
KW   Hydrolase {ECO:0000313|EMBL:ABF89324.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036685-1};
KW   Protease {ECO:0000313|EMBL:ABF89324.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW   Zinc {ECO:0000256|PIRSR:PIRSR036685-1}.
FT   DOMAIN          192..384
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   BINDING         211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036685-1"
FT   BINDING         226
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036685-1"
FT   BINDING         261
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036685-1"
FT   BINDING         288
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036685-1"
FT   BINDING         366
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036685-1"
FT   DISULFID        333..337
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036685-2"
SQ   SEQUENCE   402 AA;  42761 MW;  EE4E96CC54E5011B CRC64;
     MPVSLLLLNA PLALAEPLKA KPTDKTVWIA IGTDAITPMQ ETFAAEGWNV PTALKQQKHA
     GVFQLKESQL SRLALMMHEK FDRCAGFITY ETQEEALASL APVAPNAAQK AVSYTLTNAA
     TVNTLVGELS AANIRTTIAD LSAFPTRSQS SQGGVDAAAM LLAKWQGYVT GAGRTDVTVA
     YYPHTGWRQP SVILTIPGTD LSGEVVVVGG HLDSISSTSA APGADDDASG IATFTEVIRA
     AMARNYRPQR TVKFMAYAAE ETGLRGSREI ALSHKNNNIN VVGVMQLDMT NYKHPNATSD
     VGIVTDNTNA TQNQFIRDLI TTYVGVPFTN TTCGYGCSDH ASWHSQGYAA SIPFEGTVVQ
     KNPNIHTPRD TLANSDSSAA HALKFSKIAA AYVAELAKGT AQ
//
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