ID   A0KX67_SHESA            Unreviewed;       619 AA.
AC   A0KX67;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Peptidase M2, peptidyl-dipeptidase A {ECO:0000313|EMBL:ABK48386.1};
GN   OrderedLocusNames=Shewana3_2156 {ECO:0000313|EMBL:ABK48386.1};
OS   Shewanella sp. (strain ANA-3).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=94122 {ECO:0000313|EMBL:ABK48386.1, ECO:0000313|Proteomes:UP000002589};
RN   [1] {ECO:0000313|Proteomes:UP000002589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANA-3 {ECO:0000313|Proteomes:UP000002589};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA   Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000469; ABK48386.1; -; Genomic_DNA.
DR   RefSeq; WP_011717109.1; NC_008577.1.
DR   AlphaFoldDB; A0KX67; -.
DR   STRING; 94122.Shewana3_2156; -.
DR   KEGG; shn:Shewana3_2156; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_6; -.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000002589; 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   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_5002625622"
SQ   SEQUENCE   619 AA;  68899 MW;  112F29697480866B CRC64;
     MAILLNRPTT LALTIALTLG VTACNDAQSK AETTAAPAAT NAAPDKAQAI AFIQDAEAQM
     AQLSIEANRA EWIYSNFITE DTAALSAAVG EKVSAASVKF ATEAAKYANV ELDPANARKL
     NILRSALVLP APLDPAKNAE LAQISSELNG LYGKGKYCFA DGKCMTQPEL SSLMAESRDP
     AKLLEAWKGW REIAKPMRPL FQREVELANE GAKDLGYANL SELWRSQYDM KPDEFSQELD
     RLWGQVKPLY ESLHCYVRGE LNNEYGDAIA PKTGPIPAHL LGNMWAQQWG NVYDLVAPDD
     ADPGYDVTEL LEQKGYDEHK MVKQAESFFT SLGFAPLPDS FWSRSLFLQP KDRDVVCHAS
     AWDLDNLDDI RIKMCIQKTA EDFTVIHHEL GHNFYQRAYK QQPFLFKNSA NDGFHEAIGD
     TIALSITPSY LKQIGLLEDV PDASKDIGLL LKQALDKIAF LPFGLMIDQW RWKVFSGEIT
     PAQYNQAWWE LREKYQGVKA PTDRSEADFD PGAKYHVPGN VPYTRYFLAH ILQFQFHKAL
     CDTAGDKGPV HRCSIYGNQA AGEKLNKMLE LGASQPWPVA LKEVTGTKGM DAKAVLDYFA
     PLKTWLDEQN TAANRQCGW
//