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
//