ID A0A0A2N6B2_9FLAO Unreviewed; 437 AA.
AC A0A0A2N6B2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=D-Ala-D-Ala carboxypeptidase {ECO:0000313|EMBL:KGO95990.1};
GN ORFNames=Q767_06915 {ECO:0000313|EMBL:KGO95990.1};
OS Flavobacterium enshiense DK69.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1107311 {ECO:0000313|EMBL:KGO95990.1, ECO:0000313|Proteomes:UP000030149};
RN [1] {ECO:0000313|Proteomes:UP000030149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK69 {ECO:0000313|Proteomes:UP000030149};
RA Zeng Z., Chen C.;
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGO95990.1, ECO:0000313|Proteomes:UP000030149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK69 {ECO:0000313|EMBL:KGO95990.1,
RC ECO:0000313|Proteomes:UP000030149};
RX PubMed=26561515; DOI=10.1186/s40793-015-0084-z;
RA Zeng Z., Chen C., Du H., Wang G., Li M.;
RT "High quality draft genomic sequence of Flavobacterium enshiense DK69(T)
RT and comparison among Flavobacterium genomes.";
RL Stand. Genomic Sci. 10:92-92(2015).
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:KGO95990.1}.
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DR EMBL; JRLZ01000005; KGO95990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2N6B2; -.
DR STRING; 1107311.Q767_06915; -.
DR PATRIC; fig|1107311.5.peg.2582; -.
DR eggNOG; COG1680; Bacteria.
DR Proteomes; UP000030149; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR PANTHER; PTHR46825:SF7; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR Pfam; PF00144; Beta-lactamase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:KGO95990.1};
KW Hydrolase {ECO:0000313|EMBL:KGO95990.1};
KW Protease {ECO:0000313|EMBL:KGO95990.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030149};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..437
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001992316"
FT DOMAIN 45..332
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 437 AA; 49218 MW; AA045665856962EF CRC64;
MIRKIIICLF VISCLSISAQ ENARFRKIDS LLIYLNHNNR FMGQLSIREG DDVVFEKAYG
LPMAKKEEQP NKNTKYKIGS VTKTFTAVMI MQLIEEKRLK LDQTLSKFYP QIPNADKITI
NDLLRHRSGI VDYVNADSTT SMTASVGKKE MLAKIAAYKP LFAPNSKAEY SNSNYYLLGC
IVEDITKTPY KDNLKTRIVD RLKLKNTYIV NNVDPKRNEA PSYTYKGEQW EAVPEWDMSL
PFAAGSISST ANDLTTLLRG IFNGKLLKPT SVDEMTQLKE SYGIGLVTFP FGERKFFGHT
GGIEGYKSVV GYYPAEKLGI SLIVNGDNYN RNDIMIGILS IYYKMPYTFP NLKTVKVDEK
ILKSYEGTYS SKEIPLKINI KVDKGQIIAQ ATGQGAFTLN AVSETEFVFD PAGVNMTFGQ
KTMVLKQGGM EIKFTKE
//
