ID   A0A0N1C1M0_9SPHN        Unreviewed;       604 AA.
AC   A0A0N1C1M0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Peptidyl-dipeptidase {ECO:0000313|EMBL:KPF91950.1};
GN   ORFNames=IP81_07790 {ECO:0000313|EMBL:KPF91950.1};
OS   Novosphingobium sp. AAP83.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1523425 {ECO:0000313|EMBL:KPF91950.1, ECO:0000313|Proteomes:UP000037998};
RN   [1] {ECO:0000313|EMBL:KPF91950.1, ECO:0000313|Proteomes:UP000037998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP83 {ECO:0000313|EMBL:KPF91950.1,
RC   ECO:0000313|Proteomes:UP000037998};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPF91950.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LJHY01000016; KPF91950.1; -; Genomic_DNA.
DR   RefSeq; WP_054107416.1; NZ_LJHY01000016.1.
DR   AlphaFoldDB; A0A0N1C1M0; -.
DR   STRING; 1523425.IP81_07790; -.
DR   PATRIC; fig|1523425.4.peg.739; -.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000037998; Unassembled WGS sequence.
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:UP000037998};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..604
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005867671"
SQ   SEQUENCE   604 AA;  66231 MW;  26AD160C9FB84629 CRC64;
     MKKFVSVLAI ATATAGLATP ALAQSTATPA VVFDWVKKAE AAILADIVVG SRSGWIYSTN
     ITYDTESLVA DTGAASTAMQ VANAKQAAEY AKVSGLAPDI ARKLVMIRTQ ITGPAPSTPG
     AALEGATLQA RLQGIYGKGS GTLQGKPING SDIEAAMGTN RNPDELREMW LSWNDNVGKP
     MKADYARMVE IGNAGAEELG FADTGVLWRS NYDMSDEQFA ALTEKIWSEV KPLYDQLHCY
     TRLKLNEKYG DAVQAKTGPI RADLLGNMWA QEWGNIYDVV APAGAGDIGY DTSELLTAKG
     YDPIKMVQAG EGFYSSLGLS PMPQTFWQRS QFVKPRDRDV VCHASAWNLD NVDDLRIKMC
     IKVNGDDFVT IHHELGHNYY QRAYNKQDAL YQGGANDGFH EAIGDFVALS ITPEYLVQIG
     LLDRDKVPPA SKDTGLLLRQ AMDKIAFLPF GLLIDRWRWD VFAGKIAPAD YQAGWDAMRL
     KYQGLVPPAA RPADAFDAGA KYHVPANVPY TRYFLARVLQ FQFYEAACKQ AGWKGPLHRC
     SFYGNKDVGA KLNAMLEMGA SKPWPDALEA FTGTREMSGK AMIRYFAPLT KWLAQQTKGQ
     TCSW
//