ID A0A3S2X8M2_9BACI Unreviewed; 678 AA.
AC A0A3S2X8M2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=EM808_12055 {ECO:0000313|EMBL:RVT62518.1};
OS Niallia taxi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=2499688 {ECO:0000313|EMBL:RVT62518.1, ECO:0000313|Proteomes:UP000288024};
RN [1] {ECO:0000313|EMBL:RVT62518.1, ECO:0000313|Proteomes:UP000288024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M5HDSG1-1 {ECO:0000313|EMBL:RVT62518.1,
RC ECO:0000313|Proteomes:UP000288024};
RA Tuo L.;
RT "Bacillus sp. M5HDSG1-1, whole genome shotgun sequence.";
RL Submitted (JAN-2019) 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:RVT62518.1}.
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DR EMBL; RZTZ01000004; RVT62518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S2X8M2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000288024; 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.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000288024}.
FT DOMAIN 44..159
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 168..329
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 362..655
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 678 AA; 76185 MW; 01C046E5616BC9C9 CRC64;
MNSRVENNRR SFKPLLLFLV VIVIVFGATA SYLIIKKNDK ALFEEAAANF IRILENKDYK
KLGKALDEHS YKSLNYTLEE VEEKYDRIFN GINITDIHAS HVSLEKVNNN LYELSYQLSF
TTPLGALEKL EYKTEMTKKD DKYLVNWEPA LIFPGMEGKD KISYQYLKAE RGEIQDHLGN
GLAINETFKS MGVVAKELGE GNEKEAKLQK ISQQFDLSME EINKKLNQSW VTDELFVPLK
TIESNKAVEL PGVSYQNIKL RYYPLKEAAA NLIGYIGKVT KEDNEKHPNL VDGDIIGKAG
LEKAFDKRLR GKDGGEIWIV DENGENKQEI QTVEKADGED IQLTIDSYIQ SEAFEHLKGN
AGSTVVMNPK EGGLFALVSS PSYDPNKMVQ GISQQDYDQF ANDEKKPFIS RFAVGYAPGS
TFKTITASIG LDANVTYPDK LRTINGRSWK KDGSWGGYSV TRVSDVQNVD MRKALIYSDN
IYFAQEVLEL GEDAFRDGLK KFIFGEELDL PIAMNPAQIS KENTFNSEIL LADTAYGQGE
LLINPIQQAV MYTVFQNEGK IVYPTLVKSK ESPKTKSAIT STTANEMEKS LIEVVSNPNG
TAHLLYNKRY QLAGKTGTAE LKLKQGEKGN ENSFLLAFDT EQDNFLLLSL VEGYSKGSSA
TQLNKSFIEK LYVYFGMQ
//
