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Database: UniProt
Entry: A0A077LKC6_9PSED
LinkDB: A0A077LKC6_9PSED
Original site: A0A077LKC6_9PSED 
ID   A0A077LKC6_9PSED        Unreviewed;       485 AA.
AC   A0A077LKC6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:BAP44586.1};
GN   ORFNames=PSCI_3884 {ECO:0000313|EMBL:BAP44586.1};
OS   Pseudomonas sp. StFLB209.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1028989 {ECO:0000313|EMBL:BAP44586.1, ECO:0000313|Proteomes:UP000031652};
RN   [1] {ECO:0000313|EMBL:BAP44586.1, ECO:0000313|Proteomes:UP000031652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StFLB209 {ECO:0000313|EMBL:BAP44586.1,
RC   ECO:0000313|Proteomes:UP000031652};
RX   PubMed=25323715; DOI=10.1128/genomeA.01037-14;
RA   Morohoshi T., Kato T., Someya N., Ikeda T.;
RT   "Complete Genome Sequence of N-Acylhomoserine Lactone-Producing Pseudomonas
RT   sp. Strain StFLB209, Isolated from Potato Phyllosphere.";
RL   Genome Announc. 2:e01037-e01014(2014).
CC   -!- SIMILARITY: Belongs to the peptidase S13 family.
CC       {ECO:0000256|ARBA:ARBA00006096}.
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DR   EMBL; AP014637; BAP44586.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A077LKC6; -.
DR   STRING; 1028989.PSCI_3884; -.
DR   KEGG; pses:PSCI_3884; -.
DR   HOGENOM; CLU_017692_2_1_6; -.
DR   Proteomes; UP000031652; 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:BAP44586.1};
KW   Hydrolase {ECO:0000313|EMBL:BAP44586.1};
KW   Protease {ECO:0000313|EMBL:BAP44586.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031652};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..485
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001720987"
SQ   SEQUENCE   485 AA;  52539 MW;  3B782702BF0B4F82 CRC64;
     MRPLLLASVL LPFAFQVHAA PINTTLPPKV QQALKASKLT DDALSLVTIP LTGPGTPTVF
     NADVSVNPAS TMKLVTTFAA LEILGPTHQW KTEFFTDGTL SNGVLRGNLY LKGGGDPKLN
     MEKLWLLMRD LRANGVQQVT GDLILDRSHF VQPQLPVFDD DGGDHSKPFL VRPDSLLVNL
     KALRFVTRND DGRILVAVEP PIATIRIDNQ VKNIAAKQCG DDVRYNPVPQ ADGSLLVQVT
     GQLAKGCNSQ TYLSLLDHQA YAAGAVRAIW QELGGSIQGA DKVGNVPSGA KLLARAFSPD
     LVEVIRDINK YSNNTMAQQL FLSLGQEFRT SADGDDAKAA QRVIRQWLAK KGITAPHLVM
     ENGSGLSRAE RVSAREMAVL LQAAWRSPYA AEFTSSMPLA GMDGTMRKRL KRTPLLGEAH
     IKTGTLNTVR AIAGYSRDSN GNTWAVVAIL NDPRPFGASS VLDEVLVDLY RQPKLNATTV
     SIQQP
//
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