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Database: UniProt
Entry: K9YID8_HALP7
LinkDB: K9YID8_HALP7
Original site: K9YID8_HALP7 
ID   K9YID8_HALP7            Unreviewed;       263 AA.
AC   K9YID8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=D-Ala-D-Ala carboxypeptidase {ECO:0000313|EMBL:AFZ45873.1};
GN   OrderedLocusNames=PCC7418_3769 {ECO:0000313|EMBL:AFZ45873.1};
OS   Halothece sp. (strain PCC 7418) (Synechococcus sp. (strain PCC 7418)).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Halothecacae; Halothece cluster; Halothece.
OX   NCBI_TaxID=65093 {ECO:0000313|EMBL:AFZ45873.1, ECO:0000313|Proteomes:UP000010481};
RN   [1] {ECO:0000313|Proteomes:UP000010481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7418 {ECO:0000313|Proteomes:UP000010481};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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DR   EMBL; CP003945; AFZ45873.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9YID8; -.
DR   STRING; 65093.PCC7418_3769; -.
DR   KEGG; hao:PCC7418_3769; -.
DR   PATRIC; fig|65093.3.peg.3978; -.
DR   eggNOG; COG1876; Bacteria.
DR   HOGENOM; CLU_054193_6_1_3; -.
DR   Proteomes; UP000010481; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd14852; LD-carboxypeptidase; 1.
DR   Gene3D; 3.30.1380.10; -; 1.
DR   InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR   InterPro; IPR003709; Pept_M15B.
DR   PANTHER; PTHR34385; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR34385:SF2; PEPTIDASE M15B AND M15C; 1.
DR   Pfam; PF02557; VanY; 1.
DR   SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:AFZ45873.1};
KW   Hydrolase {ECO:0000313|EMBL:AFZ45873.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:AFZ45873.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010481};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        31..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          120..249
FT                   /note="Peptidase M15B"
FT                   /evidence="ECO:0000259|Pfam:PF02557"
FT   REGION          62..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   263 AA;  29129 MW;  0FF2A1F61E80AA60 CRC64;
     MSVGKNQPAP DEIPEALRDV TPVMEAKRTR FWLWLGSGVG LAVLGSIVGL YLWNENSKLS
     VASSPQEVET VTPKTEKKET AEAQTESSST AATPPDLLGH LPYESAPKES LTPVTADGRI
     QLRTPAAQAF IKMQNEARRE GISLVPLSGF RSIAQQEKLF FGVKAQRRQR TTERAEVSAP
     PGYSEHHTGY AIDIGDGKAP ATHVETSFGE TEAFAWLEEN AARYSFELSF PENNAQGISY
     EPWHWRYVGN QESLEIFYKN QSK
//
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