ID D4ZKU4_SHEVD Unreviewed; 612 AA. AC D4ZKU4; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAR-2024, entry version 55. DE SubName: Full=Zinc-dependent metallopeptidase {ECO:0000313|EMBL:BAJ02293.1}; GN OrderedLocusNames=SVI_2322 {ECO:0000313|EMBL:BAJ02293.1}; OS Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=637905 {ECO:0000313|EMBL:BAJ02293.1, ECO:0000313|Proteomes:UP000002350}; RN [1] {ECO:0000313|Proteomes:UP000002350} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12 RC {ECO:0000313|Proteomes:UP000002350}; RX PubMed=20458400; DOI=10.1039/c000396d; RA Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E., Toyonaga H., RA Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M., Kato C., Oshima T., RA Nakasone K., Mori H.; RT "Complete genome sequence and comparative analysis of Shewanella violacea, RT a psychrophilic and piezophilic bacterium from deep sea floor sediments."; RL Mol. Biosyst. 6:1216-1226(2010). 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; AP011177; BAJ02293.1; -; Genomic_DNA. DR RefSeq; WP_013051597.1; NC_014012.1. DR AlphaFoldDB; D4ZKU4; -. DR STRING; 637905.SVI_2322; -. DR KEGG; svo:SVI_2322; -. DR eggNOG; COG1164; Bacteria. DR HOGENOM; CLU_014364_3_0_6; -. DR OrthoDB; 5241329at2; -. DR Proteomes; UP000002350; 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. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Reference proteome {ECO:0000313|Proteomes:UP000002350}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..23 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 24..612 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5005342883" SQ SEQUENCE 612 AA; 68806 MW; 999D1F19155C0048 CRC64; MSLLMPKLSR LSLLIALSIG VSACNSSKND DSNSASSKTS EAKQFLIQSE QTLSDLSIEI NRAEWIYSNF ITDDTAALSA SAAEKLTATS VRLATQAAQY TDLALDDTSL RKLNILRSSL VLPAPLDPEK NAELAGISAQ LNGLYGKGKY CFDDGRCLTQ PELSAIMAES SDPKLLLEVW QGWREIAKPM RPLFQREVEL ANEGAKDLGY ADLSVLWRSQ YDMKPDEFSN ELDRLWGQVK PLYDSLHCYV RGELNEEYGD EVVPANGPIP AHLLGNMWAQ SWGNVYDKVS PQDADPGYDL TQLLAEHDYD EVKMVKQAES FFSSLGFDEL PDSFWERSLF VQPKDRDVVC HASAWDLDNL DDIRIKMCIQ KTAEDFTVIH HELGHNYYQR AYKNQPFIFK NSANDGFHEA IGDTIALSIT PSYLKQIGLL DEVPDASKDI GLLLKQALDK VAFMPFGLMI DQWRWKVFSG EITPDQYNQA WWDLREKYQG VKAPIERSEA DFDPGAKYHV PGNVPYTRYF LAHILQFQFH KSLCETAGDT GPVHRCSIYG NKAAGSKLNT MLEMGLSRPW PDALKVVTGS PEMDASAVLD YFAPLQVWLN EQNTQAKRQC GW //