ID   G8PJG6_PSEUV            Unreviewed;       596 AA.
AC   G8PJG6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Angiotensin I converting enzyme isoform 2 {ECO:0000313|EMBL:AEV34872.1};
GN   OrderedLocusNames=PSE_0360 {ECO:0000313|EMBL:AEV34872.1};
OS   Pseudovibrio sp. (strain FO-BEG1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Stappiaceae; Pseudovibrio.
OX   NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV34872.1, ECO:0000313|Proteomes:UP000005634};
RN   [1] {ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA   Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT   interacting bacteria.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEV34872.1, ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV34872.1,
RC   ECO:0000313|Proteomes:UP000005634};
RX   PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA   Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT   for symbiosis.";
RL   Environ. Microbiol. 15:2095-2113(2013).
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DR   EMBL; CP003147; AEV34872.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8PJG6; -.
DR   STRING; 911045.PSE_0360; -.
DR   KEGG; psf:PSE_0360; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_5; -.
DR   Proteomes; UP000005634; 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   Signal {ECO:0000256|ARBA:ARBA00022729}.
SQ   SEQUENCE   596 AA;  67248 MW;  7A237FF92FB504CD CRC64;
     MLPALSLALI PLSAAQAEGE KAVTVEDAKA FIESSEKAIQ EIGEEAGRIA WVNANFITYD
     TNWLNALMSE RTTKLYVSLA NQTKQFDGLA LPPDLARKMK LLKLNLTLPA PENDPAKIKK
     LAQINTEMET IYGTGKYEID GEALSLSKLS RIMATSRDYD KLLEVWKGWR TVSPPMKDMY
     AEMVGIANQG SSELGFKDTG SMWRSKYDMD PDDFRQDVDR LWGEVKPLYD SLHCYVRGKL
     VDHYGADKVP ADGPIPAHLL GNMWAQSWGN IYPLVAAEGD DQGYDLTKLL EEQNYTPLKM
     VQTAEGFFTS LGFDPLPETF YERSLITEPR DRDVQCHASA WNVDGKEDLR IKMCTEVTGE
     DFNTVHHELG HNFYQRAYNH QSPMYQDDPN DGFHEAIGDM VSLSITPKYL KQIGLLPLDA
     SEEVNTNILM AQALDKIAFL PFGLLVDQWR WKVFNGELTP DTYNEGWWEL REKYQGVAAP
     VERAADAFDP GAKYHIPNNV PYTRYFLAHI FQFQFYREAC RIAGWEGPLA ACSIYGNKEV
     GKKFNAMLET GSALPWQDSL EAFTGSREAD ATAILEYFAP LKAYLDEQNK GKSCGW
//