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Database: UniProt
Entry: A0A3A1R5Q2_9BACI
LinkDB: A0A3A1R5Q2_9BACI
Original site: A0A3A1R5Q2_9BACI 
ID   A0A3A1R5Q2_9BACI        Unreviewed;       664 AA.
AC   A0A3A1R5Q2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=D3H55_06330 {ECO:0000313|EMBL:RIW36072.1};
OS   Bacillus salacetis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2315464 {ECO:0000313|EMBL:RIW36072.1, ECO:0000313|Proteomes:UP000265801};
RN   [1] {ECO:0000313|EMBL:RIW36072.1, ECO:0000313|Proteomes:UP000265801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKP7-4 {ECO:0000313|EMBL:RIW36072.1,
RC   ECO:0000313|Proteomes:UP000265801};
RA   Daroonpunt R., Tanasupawat S., Yiamsombut S.;
RT   "Bacillus saliacetes sp. nov., isolated from Thai shrimp paste (Ka-pi).";
RL   Submitted (SEP-2018) 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   -!- 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:RIW36072.1}.
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DR   EMBL; QXIR01000006; RIW36072.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A1R5Q2; -.
DR   OrthoDB; 9766847at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000265801; 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   GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
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   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR007887; MecA_N.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   PANTHER; PTHR30627:SF25; PENICILLIN-BINDING PROTEIN 3; 1.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   Pfam; PF05223; MecA_N; 1.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF54427; NTF2-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..664
FT                   /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039010836"
FT   DOMAIN          24..148
FT                   /note="NTF2-like N-terminal transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF05223"
FT   DOMAIN          155..317
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          352..661
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   664 AA;  74181 MW;  CABDC0B9DC05020A CRC64;
     MKKFVFISIL MSLIFLAGCQ EKPQPDERLE AYVKLWNDQE FAEMHSGYLS QSAKETYSEE
     EFSERAKDLY TDLEVKNLQV KFDKPEEEQE WDDQESATFP VEIKMTTLAG DIQYEKEVEL
     VKETKEDQEN WYLNWDPSLI LPDLEQGDKV RIQTVPAERG DIKDREGIAL AVNGQAYEIG
     VVPEKFDKAN MQKVADLLET TPDYIEEQMN QSWVQPEHFV PLKKIPMTNR DLAVELTSIT
     GVFNQKVEAR EYPYGEATAH IIGYTGKITA EEYEELKDKG YSDQAVIGKR GLEELFEEKL
     RGTDGKVILI EKESGDAVTI ATKEVKQGED VKLTIDANLQ KELYEQMKDE TGTAAALNPN
     TGEVLSMISV PSFDPNEFAL GISSTKYKAL QDNPDQPLLN RVVNAYSPGS TMKPITAAIG
     LNSGKLDPAK AYTIEGKQWQ KDESWGGYKV TRVFDNDTKV DLESALKFSD NIYFARAGLD
     MGADTFQQGL KNFGFGEDIP FAYPITASQI TNEGEINKEI LLADSAYGQG QILMSVLHLT
     SSYGAIINDG IMMKPLLIAG AEQEVWKNDL LSKENAELLK TDLRKVVTEG IAGKAAVEGK
     AIAGKTGTAE IKSEQGTTGT ENGLFVSYDQ DNPEFVLAML LENVEDRGGS THTVEVTKKF
     YQNW
//
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