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Database: UniProt/TrEMBL
Entry: E3FP93_STIAD
LinkDB: E3FP93_STIAD
Original site: E3FP93_STIAD 
ID   E3FP93_STIAD            Unreviewed;       604 AA.
AC   E3FP93;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=Peptidyl-dipeptidase A {ECO:0000313|EMBL:ADO71903.1};
DE            EC=3.4.15.1 {ECO:0000313|EMBL:ADO71903.1};
GN   OrderedLocusNames=STAUR_4119 {ECO:0000313|EMBL:ADO71903.1};
OS   Stigmatella aurantiaca (strain DW4/3-1).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Archangiaceae; Stigmatella.
OX   NCBI_TaxID=378806 {ECO:0000313|EMBL:ADO71903.1, ECO:0000313|Proteomes:UP000001351};
RN   [1] {ECO:0000313|EMBL:ADO71903.1, ECO:0000313|Proteomes:UP000001351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO71903.1,
RC   ECO:0000313|Proteomes:UP000001351};
RX   PubMed=21037205; DOI=10.1093/molbev/msq292;
RA   Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA   Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA   Sogaard-Andersen L.;
RT   "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL   Mol. Biol. Evol. 28:1083-1097(2011).
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DR   EMBL; CP002271; ADO71903.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3FP93; -.
DR   STRING; 378806.STAUR_4119; -.
DR   KEGG; sur:STAUR_4119; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_7; -.
DR   OMA; FTVIHHE; -.
DR   Proteomes; UP000001351; 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:ADO71903.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000313|EMBL:ADO71903.1};
KW   Protease {ECO:0000313|EMBL:ADO71903.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..604
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003169663"
SQ   SEQUENCE   604 AA;  68263 MW;  816991793B4FEF0B CRC64;
     MLPLLRAACA AVALLALPSA AQQGKATPEE AKQFVERLNA DLKRLWTKQA TAEWIKSTYI
     TDDTERNAAS INEEVLAYLN QAIKDSRRFD GLKLDPDTAR MIHLLKVNSA IAAPSDAQKR
     SELASSAAKL EGLYGKGKYC SKDKAGKELC RDLGQLSDVM ASSRNYDELL DVWVGWHSIA
     PPMRPLYERF VALGNEGAKE IGFANIGNLW KSAYDMPPEQ FEQDTQRLWQ QVKPLYDELH
     CYVRARLAKK YGADKVPAGK PIPAHLLGNM WAQEWNNIYP LVEPYAGQAS LDVSAAIQKQ
     RYDAKKMVQL GEKFFTSLGL KPLPATFWER SQFTQPRDRD VVCHASAWDV TYDNDLRIKM
     CIKPTEEDLV TIHHELGHDY YFTYYYTLPV LYQSGAHDGF HEAIGDAITL SITPGYLQQA
     GLLKSVPRND KNLINLQLKD ALEKVAFLPF GLLIDQWRWD VFAGKTAPED YNKAWWALRE
     KYQGVAAPVA RSEKDFDPGA KYHVPANVPY TRYFLARILQ FQFHKAMCEA AGHQGALHEC
     SVYGNKEAGK RLQAMLEMGA SKPWPEALQA MTGQRQMDAT PLLDYFSPLR SWLKEQNKGQ
     QCGW
//
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