ID   Q2IJG3_ANADE            Unreviewed;       614 AA.
AC   Q2IJG3;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Peptidyl-dipeptidase A {ECO:0000313|EMBL:ABC81794.1};
DE            EC=3.4.15.1 {ECO:0000313|EMBL:ABC81794.1};
GN   OrderedLocusNames=Adeh_2024 {ECO:0000313|EMBL:ABC81794.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC81794.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA   Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA   Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000251; ABC81794.1; -; Genomic_DNA.
DR   RefSeq; WP_011421076.1; NC_007760.1.
DR   AlphaFoldDB; Q2IJG3; -.
DR   STRING; 290397.Adeh_2024; -.
DR   KEGG; ade:Adeh_2024; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_7; -.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000001935; 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.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:ABC81794.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000313|EMBL:ABC81794.1};
KW   Protease {ECO:0000313|EMBL:ABC81794.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..614
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004210148"
SQ   SEQUENCE   614 AA;  68540 MW;  43A196EC13A96913 CRC64;
     MTTLPVLQLA AVLLAAAPSA PAAPPQAAAA AKPTAADAKA FVGEANAELK KLWIRWSTAE
     WIKSTYITDD TERNAAALNE DQMAYLTDAI RGAVRFQGVG ADPDTERMLM LLRIASPLPA
     PSDAAQRAEL AQLAAKLEGM YGKGKWCGAP GSAARGAEKC RDLQDLEQVM AKSRDYDALL
     DAWTGWHTIS RDMRPLYERM VTISNAGARE IGFRDLGDLW RSGYDMPPDA FEADTDRLWA
     QVKPFYEELH CYVRSKLQRA YGKARVPDGK PIPAHLLGNM WAQDWANLYP LVEPYHGQPS
     LDVDAALRRQ KTDPIKMVKL GEAFFTSLGF EPLPKTFWER SQFTKPRDRD VVCHASAWDV
     TYSADLRIKM CIRPTEEDLV TIHHELGHNF YQRAYVHLPV LFQNGANDGF HEAIGDAIAL
     SITPGYLKQV GLIQTVPKDE KGVVNVQMKR ALEKVAFLPF GKLIDQWRWD VFSGKTPPSR
     YNAAWWELRR KYQGVDAPVS RSEADFDPGA KYHVPANVPY TRYFLAHVYQ FQFHKALCEA
     AGWKGPLHEC SIYGSKAAGK KLEAMLAMGA SKPWPDAYEA LTGSRQADAS AMLEYFAPLR
     AWLRKQTAGQ SCGW
//