ID A0A1U7Q076_9FLAO Unreviewed; 484 AA.
AC A0A1U7Q076;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase / D-alanyl-D-alanine-endopeptidase (Penicillin-binding protein 4) {ECO:0000313|EMBL:SIT97670.1};
GN ORFNames=SAMN05660493_02395 {ECO:0000313|EMBL:SIT97670.1};
OS Epilithonimonas bovis DSM 19482.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Epilithonimonas.
OX NCBI_TaxID=1121284 {ECO:0000313|EMBL:SIT97670.1, ECO:0000313|Proteomes:UP000187261};
RN [1] {ECO:0000313|Proteomes:UP000187261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19482 {ECO:0000313|Proteomes:UP000187261};
RA Varghese N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FTPU01000028; SIT97670.1; -; Genomic_DNA.
DR RefSeq; WP_076783809.1; NZ_FTPU01000028.1.
DR AlphaFoldDB; A0A1U7Q076; -.
DR STRING; 1121284.SAMN05660493_02395; -.
DR OrthoDB; 9802627at2; -.
DR Proteomes; UP000187261; Unassembled WGS sequence.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1.
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:SIT97670.1};
KW Hydrolase {ECO:0000313|EMBL:SIT97670.1};
KW Protease {ECO:0000313|EMBL:SIT97670.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..484
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012165623"
SQ SEQUENCE 484 AA; 53669 MW; C74F7EF9ABA8B9A7 CRC64;
MNKFRNYFSI ISIGFSSFVF SQGSVAVSTY PQVSDNQNLV KDVTAEKALL SPKDQIEFNI
NKMFTDPVLR NANWGFVVYD PKTEKIVTAY NETAPLIPAS TTKLLTTETA FSLLGTQYRW
NTQLEYSGSI DADGVLTGNL YIVGSGDPSL GGNRGGAASY GQIVSQYLDA VKEKGIKKVT
GDIIIQTAVF KENKSELPQN IVWLEQKNYY LPAGTTKDID PRNEKLIINQ SSNPFNQQKK
YFYISPYANK LVYADKYEGG WVTTKVAEPP AFLANKLRES LVRNKITVIG KVTPKIVDRD
PEPREILATY KSSTLEEIVD YTNQHSDNAY AEALLKSNGF QKLGDQTTES GRAAVTEHLK
AVGFDLNGLN YMDGSGLSKA HTVTPISQVK FLASLMKRPY YKEYLASLPI AGQTGTLRKM
FLVNSNGQIF AKTGTLNGVK CLAGYIKTRS NKTLVFSLLI NRFSGSVDQV KNRMEQLLDP
TLDL
//