ID A0A3E2JF39_9BACI Unreviewed; 610 AA.
AC A0A3E2JF39;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=D0463_10255 {ECO:0000313|EMBL:RFU64326.1};
OS Bacillus sp. V59.32b.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1758642 {ECO:0000313|EMBL:RFU64326.1, ECO:0000313|Proteomes:UP000258625};
RN [1] {ECO:0000313|EMBL:RFU64326.1, ECO:0000313|Proteomes:UP000258625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V59.32a {ECO:0000313|EMBL:RFU64326.1,
RC ECO:0000313|Proteomes:UP000258625};
RA Seuylemezian A., Vaishampayan P.;
RT "Bacillus chawlae sp. nov., Bacillus glennii sp. nov., and Bacillus saganii
RT sp. nov. Isolated from the Vehicle Assembly Building at Kennedy Space
RT Center where the Viking Spacecraft were Assembled.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
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:RFU64326.1}.
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DR EMBL; QVTC01000042; RFU64326.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2JF39; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000258625; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF32; PENICILLIN-BINDING PROTEIN 2A; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000258625};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 575..594
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..235
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 332..558
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 610 AA; 67591 MW; 57F3161B6985EDE4 CRC64;
MKGFRGIREI IPSWLIQGSF ISLSAVTIFA VGFFTFFKPE TNISNLKDQL ERSTEIYDEN
GELASKITAN KTEGISIKEM PDHVKNAVVA IEDHRFYEHN GIDYKAISRA FYTNLKAGGI
EEGGSTITQQ LTKIALLESD RTFRRKAEEY FLAREVEKEY SKDEILEMYL NQIYYGHGAW
GINKAAQVYF AKEVEELTVA EAAMLAGIIN VPSALDPYEH LNKSIDRRNL VLSRMEEHGF
ITNQEYDSAV KEEVVLDDTV PSDPLKGKYP YYVDHVLSEA SNRYDIEMDE LLTGGYKIYT
SLNQDMQKAA EKVYEDDSIF PKGTSDKLVQ SGAVLLNPKT GGIQALVGGR GEHQFLGYNR
ATQLKSSPGS TIKPLAVYAP ALEEGYEITD MLKDEKMSFG GYEPSNLGGK YKGEVPMYEA
VMNSLNVPTV WLLNEMGIGK GIDALERFGI PLDKEDRNLA IALGGGFDGV SPLDMAGAYS
TFANNGERMQ SHAILKIEDA TGKEVATWEE KKTRVTTKAV TDQITAMLLG VVEYGTGKNA
AVNEWEIAGK TGSTQLSIKG AVFYRATFAG EVDQYFWIVL AAIAIVLISA ALFGKRPAVL
EINRKHKNAQ
//
