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Database: UniProt
Entry: L5NB40_9BACI
LinkDB: L5NB40_9BACI
Original site: L5NB40_9BACI 
ID   L5NB40_9BACI            Unreviewed;       356 AA.
AC   L5NB40;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE   Flags: Fragment;
GN   ORFNames=D479_06220 {ECO:0000313|EMBL:ELK47670.1};
OS   Halobacillus sp. BAB-2008.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX   NCBI_TaxID=1246484 {ECO:0000313|EMBL:ELK47670.1, ECO:0000313|Proteomes:UP000010769};
RN   [1] {ECO:0000313|EMBL:ELK47670.1, ECO:0000313|Proteomes:UP000010769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAB-2008 {ECO:0000313|EMBL:ELK47670.1,
RC   ECO:0000313|Proteomes:UP000010769};
RX   PubMed=23469348;
RA   Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Saxena A.K.,
RA   Bagatharia S.B.;
RT   "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT   BAB-2008.";
RL   Genome Announc. 1:E00222-12(2013).
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:ELK47670.1}.
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DR   EMBL; ANPF01000021; ELK47670.1; -; Genomic_DNA.
DR   eggNOG; COG0744; Bacteria.
DR   Proteomes; UP000010769; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
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   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF32; PENICILLIN-BINDING PROTEIN 1F; 1.
DR   Pfam; PF00912; Transgly; 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:ARBA00022670};
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:UP000010769};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          64..238
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   NON_TER         356
FT                   /evidence="ECO:0000313|EMBL:ELK47670.1"
SQ   SEQUENCE   356 AA;  40150 MW;  264DE24DCB58C31D CRC64;
     MNFKKITEKL PPWSKRLKWP GIVLGSFFLL ALIGYMTILF GGRFVVEEED LILNEMTTVE
     TPDGDVIERI YTENRQVVPI SQIPEHVQEA FIAVEDSRFR DHSGVDFKGI MRAVYKDIIA
     MKKVEGASTI TQQVAKNLFL SNEKTWMRKT KEMMAASYLE RNYTKDEILE LYLNRIYFGE
     GAYGIEAASQ HYFQTSVENL TVAQGALLAG LPKAPNTYSP FDHPEEAEQR RNVVLSRMYD
     VGAIDAATMK QMQGSTLAVE KDDEEPETWS NSYVDLVIDE AADRYHISRD ELKRGGYRII
     VEMNPEIQKI AAGEMKNGEF VPGSAGEVEG AFTLMDHRTG ALVAVVGGRX XVYPVE
//
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