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Database: UniProt
Entry: A0A087AKL7_9BIFI
LinkDB: A0A087AKL7_9BIFI
Original site: A0A087AKL7_9BIFI 
ID   A0A087AKL7_9BIFI        Unreviewed;       469 AA.
AC   A0A087AKL7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KFI59317.1};
GN   ORFNames=BCUN_1658 {ECO:0000313|EMBL:KFI59317.1};
OS   Bifidobacterium cuniculi.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1688 {ECO:0000313|EMBL:KFI59317.1, ECO:0000313|Proteomes:UP000029067};
RN   [1] {ECO:0000313|EMBL:KFI59317.1, ECO:0000313|Proteomes:UP000029067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 10738 {ECO:0000313|EMBL:KFI59317.1,
RC   ECO:0000313|Proteomes:UP000029067};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S13 family.
CC       {ECO:0000256|ARBA:ARBA00006096}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFI59317.1}.
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DR   EMBL; JGYV01000026; KFI59317.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087AKL7; -.
DR   STRING; 1688.BCUN_1658; -.
DR   eggNOG; COG2027; Bacteria.
DR   Proteomes; UP000029067; Unassembled WGS sequence.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
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; 2.
DR   PRINTS; PR00922; DADACBPTASE3.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:KFI59317.1};
KW   Hydrolase {ECO:0000313|EMBL:KFI59317.1};
KW   Protease {ECO:0000313|EMBL:KFI59317.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029067};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..469
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038705279"
SQ   SEQUENCE   469 AA;  47818 MW;  5E4CB8693DCBDEE7 CRC64;
     MRRVATVIVS MLASVALAAG YVVADGNDWV DGALTFAAVD GTTFADARTV RAGTPLVAPA
     DRDKAIDAAA AAKLVDRLCA DKAVGKDVSV AVMQADGTVV SSHQPDTARE PASTMKTLTS
     LAAASVLDMG STLETRTLLA TGSDGSSTVI LSGEGDMLLG AGASDAAHVN GRAGLATLAQ
     DTAQALRKQG VTKVTVDYDD SLFGDERYPA RISENNGDQL YYTGVSSMAI DGGRQRVRPL
     DDPDTFEDYP QLSQTTAQDT AATFRTLLAA QGITVQAAAP EQVAVPEHRT ALASVSSAPL
     SAVMAFMLQH SDNTLAELFG RLLALHEGVA NSPQGATQAV LAQLDKLGVD TDGVTMADCS
     GLSPGSRLTV STLAQVQQRN LEIGIAPAAA EGLSMAGLVG TAATRLADAD ASGLLRVKTG
     SLGTVTSMAG NVSREGGGVA AFAVIVNNPS DMAGARTAVN RFVAALARL
//
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