ID A0A0N0CX25_9BACI Unreviewed; 690 AA.
AC A0A0N0CX25;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=ADM90_00740 {ECO:0000313|EMBL:KOY83971.1};
OS Lysinibacillus macroides.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=33935 {ECO:0000313|EMBL:KOY83971.1, ECO:0000313|Proteomes:UP000037977};
RN [1] {ECO:0000313|EMBL:KOY83971.1, ECO:0000313|Proteomes:UP000037977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 54 {ECO:0000313|EMBL:KOY83971.1,
RC ECO:0000313|Proteomes:UP000037977};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-2015) 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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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:KOY83971.1}.
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DR EMBL; LGCI01000002; KOY83971.1; -; Genomic_DNA.
DR RefSeq; WP_053993164.1; NZ_LGCI01000002.1.
DR AlphaFoldDB; A0A0N0CX25; -.
DR STRING; 33935.ADM90_00740; -.
DR PATRIC; fig|33935.3.peg.2992; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000037977; 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:SF11; PENICILLIN-BINDING PROTEIN 1B; 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 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 68..237
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 327..580
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 690 AA; 76981 MW; C291FB16097E2D28 CRC64;
MKRKSYHRKQ KRVKRTRKTL TFFVAFASAM IVAIVALRIY VQVAGAPPLT VPKASIFLDE
NENQIGDHFT NQRRYWVSLD EMSPYLKEAV VAVEDKDFYT HNGFDYSRIA GAILVDLKAG
SKVQGASTIT QQYARNLYLS HEKSWTRKLN EALYAYRLEV FYDKDEILEG YLNTVYYGHG
MYGVEAASRF FFGKSASDLT LAEAAMLTGV PKGPSIYSPI ANLEKATNRQ HVILKLMADQ
GAITQEEQAR AKNEQLVLKN DSWVATKSVA PYFLDVAWQE ASEILKSKNL DISEGGWTIQ
TTLNVAHQKA AEEAITKNMP ANDLQTAFVS MESKTGAVTA LVGGRDYAVS SFNRVTQAKR
QPGSTIKPIL YAAALENGYT PLTFLDVGET TFTYDNGRGT YAPKNVNGQF ADHDMSMAQA
IAISDNIYAV KTLEDIGFKE FHEMANRFNI GIGAKDNLSI ALGTVETTLY EMTNAYNILA
SQGQQTTPTT IVSIKNAHGD MIYENKDITK NQKTAISKEN AFILTEMMTG IFDPVFSDYS
PATGISIRSR MTHTYAAKSG STNSDQWLVG YTPRLTAGVW NGYDQGKNLT AKEDTAATKQ
IWIDFMETVN KGTKNEDFKK PKGVKGVVID IETGKLATDA CPKQRLVYLE EKDVPTEKCT
NFDILDSNTW GEFWNMLPFS IFKDDEKNKQ
//
