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Database: UniProt
Entry: A8LR21_DINSH
LinkDB: A8LR21_DINSH
Original site: A8LR21_DINSH 
ID   A8LR21_DINSH            Unreviewed;       495 AA.
AC   A8LR21;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Putative D-alanyl-D-alanine carboxypeptidase/endopeptidase {ECO:0000313|EMBL:ABV93944.1};
GN   OrderedLocusNames=Dshi_2208 {ECO:0000313|EMBL:ABV93944.1};
OS   Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Dinoroseobacter.
OX   NCBI_TaxID=398580 {ECO:0000313|EMBL:ABV93944.1, ECO:0000313|Proteomes:UP000006833};
RN   [1] {ECO:0000313|Proteomes:UP000006833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16493 / NCIMB 14021 / DFL 12
RC   {ECO:0000313|Proteomes:UP000006833};
RX   PubMed=19741735; DOI=10.1038/ismej.2009.94;
RA   Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I.,
RA   Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., Han C.,
RA   Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., Liebl W.,
RA   Liesegang H., Meincke L., Pati A., Petersen J., Piekarski T.,
RA   Pommerenke C., Pradella S., Pukall R., Rabus R., Stackebrandt E., Thole S.,
RA   Thompson L., Tielen P., Tomasch J., von Jan M., Wanphrut N., Wichels A.,
RA   Zech H., Simon M.;
RT   "The complete genome sequence of the algal symbiont Dinoroseobacter shibae:
RT   a hitchhiker's guide to life in the sea.";
RL   ISME J. 4:61-77(2010).
CC   -!- SIMILARITY: Belongs to the peptidase S13 family.
CC       {ECO:0000256|ARBA:ARBA00006096}.
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DR   EMBL; CP000830; ABV93944.1; -; Genomic_DNA.
DR   RefSeq; WP_012178875.1; NC_009952.1.
DR   AlphaFoldDB; A8LR21; -.
DR   STRING; 398580.Dshi_2208; -.
DR   KEGG; dsh:Dshi_2208; -.
DR   eggNOG; COG2027; Bacteria.
DR   HOGENOM; CLU_536242_0_0_5; -.
DR   OrthoDB; 5372081at2; -.
DR   Proteomes; UP000006833; Chromosome.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR000667; Peptidase_S13.
DR   NCBIfam; TIGR00666; PBP4; 1.
DR   PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR   Pfam; PF02113; Peptidase_S13; 1.
DR   PRINTS; PR00922; DADACBPTASE3.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:ABV93944.1};
KW   Hydrolase {ECO:0000313|EMBL:ABV93944.1};
KW   Protease {ECO:0000313|EMBL:ABV93944.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006833};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..495
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002725371"
SQ   SEQUENCE   495 AA;  52068 MW;  5E76A234BCEFABC9 CRC64;
     MNRRALLSGL AAQAALLPGA ARALGSSPHP APRPDGLWRR AVPELGELLR AADLGGQTSL
     AVIDLRSGLA LESVAGGTPL PPASVAKAAT ALYGLRVLGP EHRYTTRLLA TGPIRAGRLD
     GDLILAGSGD PSLDTAALAG LADRLRAAGV SEVAGALRVQ GSALPEIRSI DPGQPDHLGY
     SPAIAGLNLN FNRVYFEWKR QGSDYAITMD ARTGALRPQV RVSSMSVQPR NLPIYTYEQR
     GAADHWTVAR DALGAEGGRW LPVRNPAAYA ADVFRTLCGA QGIRVTLGPP LAVLPDTATL
     IASHDSETLP GLLRGMLKYS TNVTAECIGL TASTALGARP DSLQASGAQM AAWHSAQLMG
     AGPIRFADHS GLGDRSRISS LDMARLLSTH GTRTALTPLL KPYLPRDASG ARMASAPAQV
     VAKTGTLNFV SGLAGYITPP SGRALAFAIF SADIDRRAAL SRAERERPEG GRAWARRARR
     LQNDLVLRWS RLYGA
//
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