ID B4CY12_9BACT Unreviewed; 869 AA.
AC B4CY12;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE Flags: Precursor;
GN ORFNames=CfE428DRAFT_1453 {ECO:0000313|EMBL:EDY21160.1};
OS Chthoniobacter flavus Ellin428.
OC Bacteria; Verrucomicrobiota; Spartobacteria; Chthoniobacterales;
OC Chthoniobacteraceae; Chthoniobacter.
OX NCBI_TaxID=497964 {ECO:0000313|EMBL:EDY21160.1, ECO:0000313|Proteomes:UP000005824};
RN [1] {ECO:0000313|EMBL:EDY21160.1, ECO:0000313|Proteomes:UP000005824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin428 {ECO:0000313|EMBL:EDY21160.1,
RC ECO:0000313|Proteomes:UP000005824};
RX PubMed=21460085; DOI=10.1128/JB.00295-11;
RA Kant R., van Passel M.W., Palva A., Lucas S., Lapidus A.,
RA Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S.,
RA Larimer F.W., Land M.L., Hauser L., Sangwan P., de Vos W.M., Janssen P.H.,
RA Smidt H.;
RT "Genome sequence of Chthoniobacter flavus Ellin428, an aerobic
RT heterotrophic soil bacterium.";
RL J. Bacteriol. 193:2902-2903(2011).
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:EDY21160.1}.
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DR EMBL; ABVL01000003; EDY21160.1; -; Genomic_DNA.
DR RefSeq; WP_006978779.1; NZ_ABVL01000003.1.
DR AlphaFoldDB; B4CY12; -.
DR STRING; 497964.CfE428DRAFT_1453; -.
DR GeneID; 78185800; -.
DR eggNOG; COG0744; Bacteria.
DR InParanoid; B4CY12; -.
DR Proteomes; UP000005824; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; 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: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:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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 Glycosyltransferase {ECO:0000313|EMBL:EDY21160.1};
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:UP000005824};
KW Transferase {ECO:0000313|EMBL:EDY21160.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..237
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 350..597
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 697..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 869 AA; 93813 MW; D9C3BFEB682731F3 CRC64;
MKARLRTLLK ITAWTTAVAV ILVATVGVVG LKVYSDYVER ADQFDLTKID GLPERSAVYD
SRGNLYGYFG GENRLSVPLD KVSLFFVNAL LAREDNRFWE HHGVDTQGVL RAFLTNLRAG
ETRQGGSTIT QQLARNACGL VKRSLDRKAL EAVLARRIEE KYPKEKILEM YVNRIYFGSG
FYGIEAASRG YFGKPATDLT LGEAATLAAL IRSPRRLSPA RDLDAASQAR NDVLSRMAEL
KMISSDEATA AEAQQLQVAS HNAMHVTDDA IMEAVEGELS TLLSPDTLEY GGLKVTMTID
PALQRLAQTA ADRRLSEIES HKGYPHPRKA DFVPDPKAEQ EKPTNYLQAA VVMIDNRTGA
IKAAVGGRDY AQSKYSRALL GKRQIGSTFK PFVYAAAFDR GLMPGTFVDD GKIAAGEYPD
IPKKWSPANS DGHYGGLEPA SYGLVHSRNT MSVRVGEFAG LPMIRGLAQK VGLSDNVPEY
PVVFLGAFET TARNLTSAYT IFPNGGVYRP SYLIAKVEDR DGHVLYQPPH AEKRIISSDT
AAMVTGILQQ VMKHGTAAKA ASLGWKKNGA GKTGTTNDFF DAWFVGYTSS LTCGVWVGMD
KPQTIMEKGY GAALALPIWV DVMREAPENE YPTAPLNEGV KMAKVTLCAV SGKLATAGCA
EQHYAYQVEL PASRVPKEYC QTHPEMTPPI AAEPTYPSAT PSGQAAPYPT SNPPMYPSGT
TYPASSTGTA VTAIRPPATS NSPSIAFGGR PLSRPAPAPI IGEAGGPSTQ YPARTVYPPA
TASTRMEPPS VAEPVTTGPV EVRRAIPVTR STEPRTSSST TPSTLPPGVT EQRIVTRTPD
GRIHTTIIRT THGGRGYRTS IRSAQDGEE
//
