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
//