ID M1WV92_9NOST Unreviewed; 639 AA.
AC M1WV92;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=RINTHM_4440 {ECO:0000313|EMBL:CCH64912.1};
OS Richelia intracellularis HM01.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Richelia.
OX NCBI_TaxID=1165095 {ECO:0000313|EMBL:CCH64912.1, ECO:0000313|Proteomes:UP000054004};
RN [1] {ECO:0000313|EMBL:CCH64912.1, ECO:0000313|Proteomes:UP000054004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HM01 {ECO:0000313|EMBL:CCH64912.1,
RC ECO:0000313|Proteomes:UP000054004};
RA Hilton J.;
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HM01 {ECO:0000313|Proteomes:UP000054004};
RA Hilton J.A., Foster R.A., Tripp H.J., Carter B.J., Zehr J.P.,
RA Villareal T.A.;
RT "Diatom-associated endosymboitic cyanobacterium lacks core nitrogen
RT metabolism enzymes.";
RL Submitted (JAN-2016) 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:CCH64912.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAIS01000202; CCH64912.1; -; Genomic_DNA.
DR RefSeq; WP_008226404.1; NZ_CAIS01000202.1.
DR AlphaFoldDB; M1WV92; -.
DR Proteomes; UP000054004; 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:SF35; 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:CCH64912.1};
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:UP000054004};
KW Transferase {ECO:0000313|EMBL:CCH64912.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..255
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 348..615
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 639 AA; 70249 MW; 1C902EDA6AEF2CC9 CRC64;
MSSSTFAKKQ SKTQASLGFE FLKGVGQVAG GTLLSITMLT SSICAGGLVG LAISFRNLPD
VRQLRNYFPS ETSYIYDIKG RLLASLHGEA NREVVTLDKI SPSLKRAVLA SEDSYFYYHH
GINPRGVGRA IVTNWNSGGV REGASTVTMQ LVKNLFLSHK RAFTRKIAEA VLAIRLEQIL
SKDDILEMYL NQVYWGHNNY GVQTAARSYF NKSAWFLTLG ESAMMAGLIQ APEQFSPFVN
MKTAKKKQKE VLGRMLYLNW ITKKEYDNAL KEKIKLGKIK SFQGSALPYI TNAVSLELAN
KFGRDALLKG GMRIQTTIDT KFQEMAENVV SQWHYNLLGK GLYKNQIALV AVDPRTHFVK
ALVGGVNSRA SEFNRATQAL RQPGSSFKPF VYYTAFATGK YSPNSKVFDT PVRYRDGNSW
YYPRNYDGSF VGAMTVRTAL SLSRNIPVIK LGKAVGMNKV VEVCRTLGIM SPMQPVTSLP
LGAIEVTPLE MAGAYATLAN YGWQSPTTLI IRITDSSGNL VLDNTPKPRL VLEPWAAAST
IDIMKSVIDD GTGKNAAIGR PAAGKTGTTS SEKDIWFVGT TPELTTAVWV GRDDNRTLGK
GATGGSMVAP IWRSFMIQAL KGLPVSNFKD SSEFVRPKN
//