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Database: UniProt
Entry: A0A2B2BT85_9BACI
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ID   A0A2B2BT85_9BACI        Unreviewed;       691 AA.
AC   A0A2B2BT85;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE            EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN   ORFNames=COJ96_18605 {ECO:0000313|EMBL:PFP25773.1};
OS   Bacillus sp. AFS073361.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2033511 {ECO:0000313|EMBL:PFP25773.1, ECO:0000313|Proteomes:UP000223997};
RN   [1] {ECO:0000313|EMBL:PFP25773.1, ECO:0000313|Proteomes:UP000223997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS073361 {ECO:0000313|EMBL:PFP25773.1,
RC   ECO:0000313|Proteomes:UP000223997};
RG   Agbiome Team Llc;
RA   Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA   Shank E.A., Bowers A.;
RT   "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT   roles of natural products in bacterial physiology.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC         transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC         substituents of D-alanine.; EC=3.4.16.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034000};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family.
CC       {ECO:0000256|ARBA:ARBA00007171}.
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:PFP25773.1}.
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DR   EMBL; NUZU01000037; PFP25773.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B2BT85; -.
DR   OrthoDB; 9770103at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000223997; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR   Gene3D; 1.10.10.1230; Penicillin-binding protein, N-terminal non-catalytic domain, head sub-domain; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30627:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 1.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000223997};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          59..297
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          345..677
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   691 AA;  78418 MW;  481E3A0B67DBA5A2 CRC64;
     MEKQKKNKSH FPIRLNILFF SVFFLFSVLI LRLGFVQIVY GENFKRDLAR KEDITISSPV
     PRGRILDRDY RIIVDNVPKS AISYTNEGFS QEVMLETAEK LAKLISKKTN KVTERDKRDF
     WIMTNPERAN AKISKKEMDL YYAKKLTDND IYKYKLERIT TDELKELTKE KLEVIALFKE
     FNSGYKFTTQ IIKNEDVTAQ ELAVVSENLQ SLPGVDTTTD WERCYAFNGT LKSVLGKVTK
     SDEGLPAEQL EYFLARDYSR NDRVGKSQLE WQYENVLHGY KSKIKNVTDK TGNVIENHPV
     SNGKKGKDLV LSIDMDLQRK IDRIIEEELW AAKRYPGTYL TDRAYVVLMN PKTGEVLAMS
     GKKIVRNNQT GRVEMEDDAL GTFTTTYNVG STVKGATILT GYKTGAIAPG TVFDDAGLKI
     RATPLKKSYA YLGRLNEINA LKLSSNVYMF HTAIRIGKGH YEYDQPLNIS SKAFDSIRDS
     FASFGLGTRT GIDLPNEQSG FKGQSYLPGY LLDLVIGQYD TYSAMQLAQY VSTIANGGYR
     MQPHVAKQML EPKEGTRELG HVVKEITPTV LNTIDMKSNW LYRVKLGFKK VMQERGGTAY
     KFFGNAPYSP AGKTGTAEAF YDGPERYRFG KEPPPVMNLS LVSYAPSSNP EIAMAVIVPW
     AYQGKKDNRA NLKIGRRVLD TYFQMKKDNH S
//
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