ID Q8EE93_SHEON Unreviewed; 619 AA.
AC Q8EE93;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 08-NOV-2023, entry version 101.
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).
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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 OMA; FTVIHHE; -.
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
//