ID E6WUZ7_PSEUU Unreviewed; 668 AA.
AC E6WUZ7;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE SubName: Full=Peptidyl-dipeptidase A {ECO:0000313|EMBL:ADV27996.1};
DE EC=3.4.15.1 {ECO:0000313|EMBL:ADV27996.1};
GN OrderedLocusNames=Psesu_2161 {ECO:0000313|EMBL:ADV27996.1};
OS Pseudoxanthomonas suwonensis (strain 11-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=743721 {ECO:0000313|EMBL:ADV27996.1, ECO:0000313|Proteomes:UP000008632};
RN [1] {ECO:0000313|EMBL:ADV27996.1, ECO:0000313|Proteomes:UP000008632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11-1 {ECO:0000313|Proteomes:UP000008632};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Siebers A.K., Allgaier M., Thelen M.P.,
RA Hugenholtz P., Gladden J., Woyke T.;
RT "Complete sequence of Pseudoxanthomonas suwonensis 11-1.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP002446; ADV27996.1; -; Genomic_DNA.
DR RefSeq; WP_013535823.1; NC_014924.1.
DR AlphaFoldDB; E6WUZ7; -.
DR STRING; 743721.Psesu_2161; -.
DR KEGG; psu:Psesu_2161; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_014364_3_0_6; -.
DR OMA; FTVIHHE; -.
DR OrthoDB; 5241329at2; -.
DR Proteomes; UP000008632; 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; -; 1.
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 SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:ADV27996.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000313|EMBL:ADV27996.1};
KW Protease {ECO:0000313|EMBL:ADV27996.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008632};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..668
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003212469"
FT REGION 645..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 74922 MW; D80AC075E90A5637 CRC64;
MNHRPLLLAI AVAAGLLSLS ACRKTPSPEQ EKPAARAENG ETADQFVARI NAEFKAAYPE
LTSAQWLSST YINDDSQLVA AKANERALAQ LNAWIEEAKK FEGQPMSDDS RRALNLLKQA
TAMPAPRDPE KLAELTRIAA KMEGAYGAGT YCSGEGAARK CRQLGELEDV LRSSRDYDAQ
LDAWAGWHSI AQPMREDYVR FVELVNEGAR ELGYADTGAM WRSGYDMEPD AFSAETDRLW
EQVRPLYEQL HCYTRDKLQQ TYGVERGVVG EGLLPAHLMG NMWQQDWGNL WDMLQPYKGV
GDLDITAALE RQYQQLLSAA LHRRDPSPGP RERFEAEREA QLAMAKAMTE RAQDFYVSLG
MPRLPESYWE KSQFIKPLDR DVVCHASAWD MNMGGADGKS PDVRTKMCIK PNEEDFTTIY
HELGHIYYDL AYNPQPPLFQ NGANDGFHEA IGDTIVLAMT PKYLESIGLV QGQAQSHEAL
INTQMRMALA KVSFLPFGLM IDRWRWGVFD GSITPDRYNQ AWWELKARYQ GVAPVQPRGE
EFFDPGAKYH VPGNTPYTRY FLAHLLQFQF YKSLCEAAGH TGPLYECSFH GSEAAGEKFR
AMLARGASQP WQATLKELTG SERIDGGAVL EYFAPLQEWL QQQNQGKSCG WQGQSAQAPK
PEAPAKAG
//