ID   A0A150AYS5_BACCE        Unreviewed;       428 AA.
AC   A0A150AYS5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   05-JUL-2017, entry version 7.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KXX89104.1};
GN   ORFNames=AT274_05575 {ECO:0000313|EMBL:KXX89104.1};
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396 {ECO:0000313|EMBL:KXX89104.1, ECO:0000313|Proteomes:UP000075591};
RN   [1] {ECO:0000313|EMBL:KXX89104.1, ECO:0000313|Proteomes:UP000075591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL W8-0275 {ECO:0000313|EMBL:KXX89104.1,
RC   ECO:0000313|Proteomes:UP000075591};
RA   Kovac J.;
RT   "Bacillus cereus Group isolate.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S11 family.
CC       {ECO:0000256|RuleBase:RU004016}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KXX89104.1}.
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DR   EMBL; LOMT01000128; KXX89104.1; -; Genomic_DNA.
DR   RefSeq; WP_000245999.1; NZ_MLKL01000002.1.
DR   ProteinModelPortal; A0A150AYS5; -.
DR   EnsemblBacteria; KXX89104; KXX89104; AT274_05575.
DR   PATRIC; fig|1396.432.peg.773; -.
DR   Proteomes; UP000075591; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR   Gene3D; 2.60.410.10; -; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR018044; Peptidase_S11.
DR   InterPro; IPR012907; Peptidase_S11_C.
DR   InterPro; IPR001967; Peptidase_S11_N.
DR   Pfam; PF07943; PBP5_C; 1.
DR   Pfam; PF00768; Peptidase_S11; 1.
DR   PRINTS; PR00725; DADACBPTASE1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:KXX89104.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000075591};
KW   Hydrolase {ECO:0000313|EMBL:KXX89104.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000313|EMBL:KXX89104.1};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     26       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        27    428       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5007808934.
FT   TRANSMEM    397    416       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       46    266       Peptidase_S11. {ECO:0000259|Pfam:
FT                                PF00768}.
FT   DOMAIN      312    376       PBP5_C. {ECO:0000259|Pfam:PF07943}.
SQ   SEQUENCE   428 AA;  47978 MW;  8137B90AABE70835 CRC64;
     MVNFKKILAF ITVICLFFLT PMTLRAETNI GVNPEQVAPP PKEGPNVFSQ FATTIDAKTG
     DILYDKNAHH RAFPASMTKV LTAILLMEHT KPEDQFTFSQ LALDQEKSNY QIEFQPGETI
     NRNTALMILM VLSANDVSYA IAERIGGSVE NFANMMNERA KQLGATDSHF VTPNGLHDPN
     HYTTPYDMAM ITRGVQKYPE ILQAMNTKRT TVTTSRQTVS IFNKSTYFEN PFSIGGKTGF
     TNEARNTLVL LNEKDGNRII NVVMASQRPE IYEDLKQMAD YSFGQFVKQT VLDKHSWHQK
     TTYLNKDIDS ELEKSAELML KKDEGKNVKT TFRAASLDKD SLYHKGIHRG EVVGAVDITK
     NNQTIATVNV LSKEDVTFAM PKKDTIEPEV NESNVKIISI GIGAAILFGA ILFVVLRRNT
     KGMKSEEK
//