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
//