ID Q8EE93_SHEON Unreviewed; 619 AA. AC Q8EE93; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 102. DE SubName: Full=Peptidase family M2 {ECO:0000313|EMBL:AAN55525.1}; GN OrderedLocusNames=SO_2494 {ECO:0000313|EMBL:AAN55525.1}; OS Shewanella oneidensis (strain MR-1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN55525.1, ECO:0000313|Proteomes:UP000008186}; RN [1] {ECO:0000313|EMBL:AAN55525.1, ECO:0000313|Proteomes:UP000008186} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR-1 {ECO:0000313|EMBL:AAN55525.1, RC ECO:0000313|Proteomes:UP000008186}; RX PubMed=12368813; DOI=10.1038/nbt749; RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., RA Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A., RA Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S., RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R., RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J., Weidman J., RA Impraim M., Lee K., Berry K., Lee C., Mueller J., Khouri H., Gill J., RA Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C., RA Nealson K.H., Fraser C.M.; RT "Genome sequence of the dissimilatory metal ion-reducing bacterium RT Shewanella oneidensis."; RL Nat. Biotechnol. 20:1118-1123(2002). 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; AE014299; AAN55525.1; -; Genomic_DNA. DR RefSeq; NP_718081.1; NC_004347.2. DR RefSeq; WP_011072459.1; NZ_CP053946.1. DR AlphaFoldDB; Q8EE93; -. DR SMR; Q8EE93; -. DR STRING; 211586.SO_2494; -. DR PaxDb; 211586-SO_2494; -. DR KEGG; son:SO_2494; -. DR PATRIC; fig|211586.12.peg.2402; -. DR eggNOG; COG1164; Bacteria. DR HOGENOM; CLU_014364_3_0_6; -. DR OrthoDB; 5241329at2; -. DR BioCyc; SONE211586:G1GMP-2279-MONOMER; -. DR Proteomes; UP000008186; 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:UP000008186}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..23 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 24..619 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004305551" SQ SEQUENCE 619 AA; 69378 MW; 4FFE269AF79596AD CRC64; MAILLNRPTT LALTIALTLN LTACNNKQNT SETKTSIPAS TSTPDKAQAI AFIQDAEAQM AQLSIEANRA EWIYSNFITE DTAALSAAVG EKVSAASVKF ATEAAKYANV ELDPANARKL NILRSALVLP APLDPAKNAE LAQISSELNG LYGKGKYCFA DGKCMTQPEL SSLMAESRDP AKLLEAWKGW REIAKPMRPL FQREVELANE GAKDLGYANL SELWRSQYDM KPDEFSQELD RLWSQVKPLY ESLHCYVRGE LNKEYGDAIA PKTGPIPAHL LGNMWAQQWG NVYDLVAPEN ADPGYDVTEL LAQKGYDEHR MVKQAESFFT SLGFAPLPDS FWSRSLFLQP KDRDVVCHAS AWDLDNLDDI RIKMCIQKTA EDFTVIHHEL GHNFYQRAYK QQPFLFKNSA NDGFHEAIGD TIALSITPSY LKQIGLLEEV PDASKDIGLL LKQALDKIAF LPFGLMIDQW RWKVFSGEIT PAQYNQAWWE LREKYQGVKA PTPRSETDFD PGAKYHVPGN VPYTRYFLAH ILQFQFHKAL CETAGDKGPV HRCSIYGNQA AGEKLNRMLE LGSSQPWPMA LKEVTGTETM DANAVLDYFA PLKTWLDEQN KAANRQCGW //