ID   Q1D6F2_MYXXD            Unreviewed;       624 AA.
AC   Q1D6F2;
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=Peptidyl-dipeptidase A {ECO:0000313|EMBL:ABF92909.1};
DE            EC=3.4.15.1 {ECO:0000313|EMBL:ABF92909.1};
GN   OrderedLocusNames=MXAN_3581 {ECO:0000313|EMBL:ABF92909.1};
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF92909.1, ECO:0000313|Proteomes:UP000002402};
RN   [1] {ECO:0000313|EMBL:ABF92909.1, 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; ABF92909.1; -; Genomic_DNA.
DR   RefSeq; WP_011553607.1; NC_008095.1.
DR   AlphaFoldDB; Q1D6F2; -.
DR   STRING; 246197.MXAN_3581; -.
DR   EnsemblBacteria; ABF92909; ABF92909; MXAN_3581.
DR   GeneID; 41360927; -.
DR   KEGG; mxa:MXAN_3581; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_7; -.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000002402; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd06461; M2_ACE; 1.
DR   Gene3D; 1.10.1370.30; -; 2.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   PANTHER; PTHR10514:SF27; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   Pfam; PF01401; Peptidase_M2; 1.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:ABF92909.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000313|EMBL:ABF92909.1};
KW   Protease {ECO:0000313|EMBL:ABF92909.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..624
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004188266"
FT   REGION          32..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   624 AA;  70037 MW;  5CD05840F8A483AA CRC64;
     MNRKRPLNSL LRAAAVMVLP AFLGCAQDSQ VTREAPTPAE SPAAASQPSP AEAKAFAEKV
     NADLKSLWTK QATAEWIKST YITDDTEQNA AFVNEEVLAY VNGAIKEARR FEGLTLDADT
     ARMLHLLKVS QALPAPSDAE RRSELAATAA KLEGLYGKGK YCGPDGKGKC RDLEVLSDVI
     AESRNFDELL DAWQGWHSVA RPMRPLYERL VSISNEGAKD IGFNDLGTLW RSAYDMSPGE
     FEVEAQRLWG QVKPLYDDLH CYVRGRLAKQ YGADKVPDGK PIPAHLLGNM WAQEWNNIYP
     LVEPFPGQAS LDVDAALKQQ KYDAMRMVKL GEKFFTSLGL KELPPSFFER SQFTKPEGRD
     VVCHASAWDV NFSNDLRIKM CIKPTEEDLV TIHHELGHNY YYTYYYQLPV LYQAGANDGF
     HEAIGDALTL SITPGYLQQA GLLKAVPKNE KNLINLQMKD ALEKIAFLPF GLLVDQWRWE
     VFSGRVQPAD YNKSWWTLRE KYQGVAAPVA RSEQDFDPGA KYHVPANVPY TRYFLARILQ
     FQFHKALCEA SGYKGALHEC SIYGNKDAGK RLQAMLELGA SKPWPDALQA MTGTRQMDAT
     PLLDYFSPLR TWLQAQNKGQ KCGW
//