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Database: UniProt/TrEMBL
Entry: A7HB92_ANADF
LinkDB: A7HB92_ANADF
Original site: A7HB92_ANADF 
ID   A7HB92_ANADF            Unreviewed;       622 AA.
AC   A7HB92;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   SubName: Full=Peptidyl-dipeptidase A {ECO:0000313|EMBL:ABS25988.1};
DE            EC=3.4.15.1 {ECO:0000313|EMBL:ABS25988.1};
GN   OrderedLocusNames=Anae109_1785 {ECO:0000313|EMBL:ABS25988.1};
OS   Anaeromyxobacter sp. (strain Fw109-5).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=404589 {ECO:0000313|EMBL:ABS25988.1, ECO:0000313|Proteomes:UP000006382};
RN   [1] {ECO:0000313|EMBL:ABS25988.1, ECO:0000313|Proteomes:UP000006382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fw109-5 {ECO:0000313|EMBL:ABS25988.1,
RC   ECO:0000313|Proteomes:UP000006382};
RX   PubMed=25614562; DOI=10.1128/genomeA.01449-14;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA   Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA   Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA   Loeffler F.E., Fields M.W.;
RT   "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT   metal-reducing bacterium isolated from a contaminated subsurface
RT   environment.";
RL   Genome Announc. 3:0-0(2015).
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DR   EMBL; CP000769; ABS25988.1; -; Genomic_DNA.
DR   RefSeq; WP_012096564.1; NC_009675.1.
DR   AlphaFoldDB; A7HB92; -.
DR   STRING; 404589.Anae109_1785; -.
DR   KEGG; afw:Anae109_1785; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_7; -.
DR   OMA; FTVIHHE; -.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000006382; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006382};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..622
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002710005"
FT   REGION          18..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   622 AA;  69146 MW;  6D076216AAECCFA7 CRC64;
     MRHILLVTAL LLSTAAGGAA AEPSDPDARA TVVAPAPSSK PPTAAEAKAF VDGVNAELKR
     LWIRSSTADW IKATYITDDT ERNAAALNED VMAYLSRAIA ESVRFDGVKA DADTARMLHL
     LKVASSLPAP SDAARRRELA EISAKLEGIY GKGKWCGTPA PGRAAPRCRD LQQLEEVLAK
     SRSYPELLDA WTGWHTISRE MRPLYERLVT LGNEGAREIG FSDLGDLWRA DYDMAPEAFE
     ADVGRLWAEV KPLYDELHCY VRGRLQQAYG KAKVPDGKPI PAHLLGNMWA QDWSNLYPLV
     EPFKGVGSLD VDAALKRQKY DAARMVKLGE AFFTSLGLEP LPPSFWERSQ LVKPRDREVV
     CHASAWDVTF AADLRIKMCI RPIEEDLVTI HHELGHNYYQ RAYVHLPLLF QDSANDGFHE
     ALGDAIALSV TPGYLKQVGL VPGVPKDDRG TINFQMKKAL EKIAFLPFGL LIDQWRWDVF
     SGKVPPDRYN AAWWELRRKY QGVDAPVARS EADFDPGAKY HIPSNVPYTR YFLAHVYQFQ
     FHQALCEAAG WKGPLHQCSI YGSKDAGKRL VAMMELGASR PWPEAYAALA GAKQADASAL
     LAYFAPLRKW LAEQNAGRTC GW
//
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