ID A0A2N0Z1N6_9BACI Unreviewed; 692 AA.
AC A0A2N0Z1N6;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=CWS01_11870 {ECO:0000313|EMBL:PKG23425.1};
OS Niallia nealsonii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=115979 {ECO:0000313|EMBL:PKG23425.1, ECO:0000313|Proteomes:UP000233375};
RN [1] {ECO:0000313|EMBL:PKG23425.1, ECO:0000313|Proteomes:UP000233375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-92 {ECO:0000313|EMBL:PKG23425.1,
RC ECO:0000313|Proteomes:UP000233375};
RX PubMed=12656168; DOI=10.1099/ijs.0.02311-0;
RA Venkateswaran K., Kempf M., Chen F., Satomi M., Nicholson W., Kern R.;
RT "Bacillus nealsonii sp. nov., isolated from a spacecraft-assembly facility,
RT whose spores are gamma-radiation resistant.";
RL Int. J. Syst. Evol. Microbiol. 53:165-172(2003).
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:PKG23425.1}.
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DR EMBL; PISE01000024; PKG23425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N0Z1N6; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000233375; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000233375};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..241
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 335..613
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT COILED 626..692
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 692 AA; 77341 MW; 797DF4406E2A7EAF CRC64;
MEKLKPYIEK IRLFWKKRHI TQIILLALLI VILLSILYFT YLASQANVST LKAGLSQATV
IYDKDGDEAT RIKTDRTEGV EISELPDYVP GAVVAIEDER FYQHNGFDIK GIARVFFKNI
LAGRITGGGS TITQQLTKNA LLSSEQTYKR KAEELFLAVE IEKHYKKDEI LQMYLNHVYF
GSGAWGIDTA SQKYFNKSIK NVSISEAALL AGLLQAPSAL DPYKNYDGAM KRRDVVLSKM
KEQNIITNKE YKKAVREKII LEDGGGSFIK REYPYYTDAV IDEAISLYGL TQDELLKRGY
KIYTEMDQNL QSTLEKTFDR DDLFPSSSDN TLVQGGAVLL DPETGGIKGL VGGRGEHVFR
GFNRATQIKA QPGSTMKPLA VYTPALEEGY KVTSKLQDKP FKKGDYEPQN FTKTYQGEVP
MYEALEKSLN VPAVWLLDKI GLDKGLDSLE RFGIPLDKED EYLGVALGGM HKGVSPLQMA
EAYSTFPNDG ERMESHLITK IVGPTGKVIA EYKSKSTKVT SKSVTDDMTS MLLDVIKTGT
GQGAQVSGFQ IAGKTGSTQL PFNATGTKDQ WFVGYTPNLV GAMWLGYDKT DQQHYLESKS
SGDVVPIFKT IMDQAVQYVE PENFSVSSVS QQLANEEDTK QKVEKTKKEI TEKAKELEGT
LRENSSKWKE VINEMKKDAE KVTEKVKEII GN
//
