ID   C7RC09_KANKD            Unreviewed;       624 AA.
AC   C7RC09;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Peptidyl-dipeptidase A {ECO:0000313|EMBL:ACV26801.1};
DE            EC=3.4.15.1 {ECO:0000313|EMBL:ACV26801.1};
GN   OrderedLocusNames=Kkor_1388 {ECO:0000313|EMBL:ACV26801.1};
OS   Kangiella koreensis (strain DSM 16069 / KCTC 12182 / SW-125).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Kangiellales; Kangiellaceae;
OC   Kangiella.
OX   NCBI_TaxID=523791 {ECO:0000313|EMBL:ACV26801.1, ECO:0000313|Proteomes:UP000001231};
RN   [1] {ECO:0000313|EMBL:ACV26801.1, ECO:0000313|Proteomes:UP000001231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16069 / KCTC 12182 / SW-125
RC   {ECO:0000313|Proteomes:UP000001231};
RX   PubMed=21304661; DOI=10.4056/sigs.36635;
RA   Han C., Sikorski J., Lapidus A., Nolan M., Glavina Del Rio T., Tice H.,
RA   Cheng J.F., Lucas S., Chen F., Copeland A., Ivanova N., Mavromatis K.,
RA   Ovchinnikova G., Pati A., Bruce D., Goodwin L., Pitluck S., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA   Saunders E., Brettin T., Goker M., Tindall B.J., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT   "Complete genome sequence of Kangiella koreensis type strain (SW-125).";
RL   Stand. Genomic Sci. 1:226-233(2009).
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DR   EMBL; CP001707; ACV26801.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7RC09; -.
DR   STRING; 523791.Kkor_1388; -.
DR   KEGG; kko:Kkor_1388; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_6; -.
DR   InParanoid; C7RC09; -.
DR   Proteomes; UP000001231; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
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   Carboxypeptidase {ECO:0000313|EMBL:ACV26801.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000313|EMBL:ACV26801.1};
KW   Protease {ECO:0000313|EMBL:ACV26801.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001231};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..624
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002983627"
SQ   SEQUENCE   624 AA;  70632 MW;  5616A733386EC5AE CRC64;
     MMKIKSAVSS AVLFSALLGL SACSDDADKQ QTNEAQQTEA QVTVADAEKF VADAEKRLSE
     ISEYGARIAW VNANFVTHDT TQLNAKVGEE YTKLGVELAN GAKQFNDLEL PYDLNRKLEM
     IKLGLTLPAP SDADKTKKLA EITSKLDSIY ATGKSPDGRN LGQLSEVLRT SRDPQEQLEA
     WLGWRTVSPE MRPLYQEMVE IANEGSKELG YKDTGAMWRS KYDMPADDFA NEMDRLWGQV
     EPLYEALHCH VRAELNEEYG DEVVALDKPI PAHLLGNMWA QQWGNIYDLV APEGATKGVD
     LDPILRKHYG VDHEVVTYNE KEKAVKKMVK TAENFFSSLG FAPLPDTFWE RSLFVKPRDR
     DVQCHASAWD IDNQEDIRIK MCTEINAEDF QTVHHELGHN YYQRAYKDQP ILYKGSANDG
     FHEAIGDTVA LSITPAYLKQ IGLIEEEPDA DADIALLMRS AMDKVAFLPF GLMVDKWRWQ
     VFNGEVSAAD YNKGWWNLRT EYQGIAPAVE RSEVDFDPGA KYHIPGNTPY SRYFLAHILQ
     FQFFRDMCEM AGNEGPLHRC SFYGNKEVGA KLNAMLEMGS SRPWQDALEA MTGQREMDAT
     AVLEYYAPLK TWLDEQNKDR NCGW
//