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Database: UniProt/TrEMBL
Entry: A0A0M5IM01_SPHS1
LinkDB: A0A0M5IM01_SPHS1
Original site: A0A0M5IM01_SPHS1 
ID   A0A0M5IM01_SPHS1        Unreviewed;       614 AA.
AC   A0A0M5IM01;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Peptidyl-dipeptidase {ECO:0000313|EMBL:ALC13561.1};
GN   ORFNames=LH20_16505 {ECO:0000313|EMBL:ALC13561.1};
OS   Sphingopyxis sp. (strain 113P3).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=292913 {ECO:0000313|EMBL:ALC13561.1, ECO:0000313|Proteomes:UP000061305};
RN   [1] {ECO:0000313|EMBL:ALC13561.1, ECO:0000313|Proteomes:UP000061305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=113P3 {ECO:0000313|EMBL:ALC13561.1,
RC   ECO:0000313|Proteomes:UP000061305};
RX   PubMed=26472829;
RA   Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA   Tsuda M., Fujita N., Kawai F.;
RT   "Complete Genome Sequence of Polyvinyl Alcohol-Degrading Strain
RT   Sphingopyxis sp. 113P3 (NBRC 111507).";
RL   Genome Announc. 3:e01169-15(2015).
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DR   EMBL; CP009452; ALC13561.1; -; Genomic_DNA.
DR   RefSeq; WP_053555123.1; NZ_CP009452.1.
DR   AlphaFoldDB; A0A0M5IM01; -.
DR   STRING; 292913.LH20_16505; -.
DR   KEGG; sphp:LH20_16505; -.
DR   PATRIC; fig|292913.6.peg.3356; -.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000061305; 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:UP000061305};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..614
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005803367"
SQ   SEQUENCE   614 AA;  67752 MW;  BEBBD5009B71D301 CRC64;
     MKAMISTLSL AISLAFAASP VMAQTAPAET AAAAAPTAAD AEAFIAAAEK DLFDYTVEAS
     QVNWVNYNFI TEDTDAMAAR INAIGTEKAV KYALEAARYR DVPGLSADTK RKLDILRNGI
     VLPAPTTEGA AAELNRIATD LSSQYGKGKG TLDGKPIAGS DIEAEMGNLE HTPAQFAEMW
     TSWHDNVGAP MKRDYAKMVG IANEGAKELG FSDVGAMWRS GYDMPPEEFA RTTERLWEEV
     KPLYLALHTY VRWKLNEKYG DAVQPKTGPI RADLLGNMWA QEWGNIYPLV APAGSGDLGY
     DIGDLLKAQG KTPLDMVKAG ENFYSSLGFA PLPETFWKRS LFVKPADREV VCHASAWNID
     NKDDVRIKMC TKVNSDDFVT IHHELGHNYY QRAYNKQPFL YLNGANDGFH EAIGDFVALS
     ITPQYLVDIG LLDKAQVPGA DKDIGLLLRQ AMDKVAFLPF GLLVDRWRWG VFDGTIQPAD
     YNKAWTDLRQ QYQGIIPPGE RPADAFDPGA KYHIPGNTPY SRYFLARILQ FQFYEAACKQ
     AGWKGPLHRC SFYGNKKVGA KLNAMLEMGA SKPWPDALEA FTGSREMSGK AMAAYFAPLK
     TWLDEQNKGK PSGW
//
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