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
//