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Database: UniProt
Entry: A0A1U7Q076_9FLAO
LinkDB: A0A1U7Q076_9FLAO
Original site: A0A1U7Q076_9FLAO 
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}.
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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
//
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