ID   A3WBI9_9SPHN            Unreviewed;       624 AA.
AC   A3WBI9;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Zinc-dependent metallopeptidase {ECO:0000313|EMBL:EAQ30434.1};
GN   ORFNames=NAP1_06640 {ECO:0000313|EMBL:EAQ30434.1};
OS   Erythrobacter sp. NAP1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=237727 {ECO:0000313|EMBL:EAQ30434.1, ECO:0000313|Proteomes:UP000002995};
RN   [1] {ECO:0000313|EMBL:EAQ30434.1, ECO:0000313|Proteomes:UP000002995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAP1 {ECO:0000313|EMBL:EAQ30434.1,
RC   ECO:0000313|Proteomes:UP000002995};
RX   PubMed=21952547; DOI=10.1128/JB.05845-11;
RA   Koblizek M., Janouskovec J., Obornik M., Johnson J.H., Ferriera S.,
RA   Falkowski P.G.;
RT   "Genome Sequence of the Marine Photoheterotrophic Bacterium Erythrobacter
RT   sp. Strain NAP1.";
RL   J. Bacteriol. 193:5881-5882(2011).
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:EAQ30434.1}.
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DR   EMBL; AAMW01000001; EAQ30434.1; -; Genomic_DNA.
DR   RefSeq; WP_007164464.1; NZ_CH672390.1.
DR   AlphaFoldDB; A3WBI9; -.
DR   STRING; 237727.NAP1_06640; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_5; -.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000002995; 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; -; 1.
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:UP000002995};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..624
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002661752"
SQ   SEQUENCE   624 AA;  69382 MW;  27FA7A207E57F3DD CRC64;
     MKFTKLSLKA SAAALAVSLA ATSVPALAEA HQDSAEMQDA GTQFPLTPEG AAQFVASVED
     EMRAFSEPYA RVSWLNATYI NTDSNALASQ YGAQLTTMSV GFANEAAKYA AVEGLDPEVE
     RKLGMLRYSI GLPAPARDGA AEELSDIATR LRAAYGAGRG TLNGEEIGGS DIEAEMGNLD
     RTPEELAEMW ASWHDNVGAP MREDYAQYVS LANEGAAELG FDDLGTMWRS GYDMSPEEFA
     ADTERMWQEV KPLYVALHTY VRRKLNEHYG DEVQPATGPI RADLLGNMWA QEWGNIYPLV
     APEGAGDIGY DLTDLIVEKD LDAVEMTRVG EQFFSSLGFE PLPQTFWERS QFTKPADREV
     VCHASAWNLD NVDDLRIKMC IKQNADDFIT IHHELGHNYY QRAYNQQDFM HLGGANDGFH
     EAIGDMIALS ITPEYLVQID MLEPEQVPSA DKDIGLLLRQ AMDKVAFLPF GLLIDRYRWS
     LFDGSVAPGD YNKAWNDIRL EYQGITPPVE RPADGFDPGA KYHVPGNVSY TRYFLARLLQ
     FQFFKAACDQ AGWEGPLHRC SFYGNEEVGK NLNAMLELGA SEPWPEALEA FTGERQMNGT
     AMVEYFAPLM AWLEEQNEGQ EEGW
//