ID   C5BJ95_TERTT            Unreviewed;       592 AA.
AC   C5BJ95;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Dipeptidyl carboxydipeptidase family protein {ECO:0000313|EMBL:ACR12366.1};
DE            EC=3.4.15.- {ECO:0000313|EMBL:ACR12366.1};
GN   OrderedLocusNames=TERTU_2099 {ECO:0000313|EMBL:ACR12366.1};
OS   Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Teredinibacter.
OX   NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR12366.1, ECO:0000313|Proteomes:UP000009080};
RN   [1] {ECO:0000313|EMBL:ACR12366.1, ECO:0000313|Proteomes:UP000009080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080};
RX   PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA   Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA   Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA   Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA   Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA   Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA   Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA   Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT   "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT   endosymbiont of marine wood-boring bivalves (shipworms).";
RL   PLoS ONE 4:E6085-E6085(2009).
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DR   EMBL; CP001614; ACR12366.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5BJ95; -.
DR   STRING; 377629.TERTU_2099; -.
DR   KEGG; ttu:TERTU_2099; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_6; -.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000009080; 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.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:ACR12366.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000313|EMBL:ACR12366.1};
KW   Protease {ECO:0000313|EMBL:ACR12366.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009080};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
SQ   SEQUENCE   592 AA;  66584 MW;  46CEEC3C718A20A9 CRC64;
     MACNQPEKGS DAAKANAEQY NEESAKAFLK EAEAELGDAS LFLNHASWLA ATYINFDSQE
     VEARAGKEFT LKTVQFAKQV KKWDGADLTP DTRRQLDGLR LALSFPAPDD EKLASELAQI
     GSKMQGMYGA GQYCMADGNC MSLGDMSKIL AESDDPELMK SVWAGWRDVS PPMRGLYERQ
     VEIANQGAQD LGYANLADLW RSNYDMQPEA FAADVDAQWD KVKPFYEALH CHVRAKLNEF
     YGDDVVPSQG KIPAHLLGNM WAQTWSNVYD KVKPEVSSSY NLTSLIEKKG MTELDMVKTG
     EAFFSSIGFE PLPETFWERS MFTKPRDRDV VCHASAWDLD DKDDLRIKMC IQKNAEDFQT
     IHHELGHNYY QRAYKEQPFI YRGSANDGFH EALGDTVALS ITPSYLVQIG LLDKEPPVDE
     DLGQLLELAL DKIAFLPFGL LVDKWRWQVF SGELAPADYN KGWWELREKY QGIAAPVARS
     EEDFDPGAKY HIPGNTPYTR YFLAFIQQFQ FHKALCETAG YEGPLHRCSI YGNEAAGAKL
     KAMMEMGSSK PWQEAMAAVT GQETLDASAI IDYFAPVKAW LDEQNKGRSC GW
//