ID F1Z4Z7_9SPHN Unreviewed; 691 AA.
AC F1Z4Z7;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=Y88_1910 {ECO:0000313|EMBL:EGD60036.1};
OS Novosphingobium nitrogenifigens DSM 19370.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=983920 {ECO:0000313|EMBL:EGD60036.1, ECO:0000313|Proteomes:UP000004728};
RN [1] {ECO:0000313|EMBL:EGD60036.1, ECO:0000313|Proteomes:UP000004728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19370 {ECO:0000313|EMBL:EGD60036.1,
RC ECO:0000313|Proteomes:UP000004728};
RX PubMed=22156397; DOI=10.1128/JB.06381-11;
RA Strabala T.J., Macdonald L., Liu V., Smit A.M.;
RT "Draft Genome Sequence of Novosphingobium nitrogenifigens Y88T.";
RL J. Bacteriol. 194:201-201(2012).
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 -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000256|ARBA:ARBA00007090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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:EGD60036.1}.
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DR EMBL; AEWJ01000023; EGD60036.1; -; Genomic_DNA.
DR AlphaFoldDB; F1Z4Z7; -.
DR STRING; 983920.Y88_1910; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_7_5; -.
DR InParanoid; F1Z4Z7; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000004728; Unassembled WGS sequence.
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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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; PENICILLIN-INSENSITIVE TRANSGLYCOSYLASE; 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 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000004728}.
FT DOMAIN 49..216
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 301..524
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 603..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 73937 MW; 33796ED8AF11A83E CRC64;
MLLAGIGLAA AVAITARSLP SYERLKSSQA GQMIVVRAAD GSEIVTLGPS YGKWIPIQRM
PRVMQDAMIS VEDRRFREHW GVDPIGIVRS VYVRVEKGRW RQGGSTITQQ LARNIFLNSN
RTFDRKIREA VLALALETKF SKDQILELYL NKVYFGGGAY GVDSAARKFF GHSGEQLSLG
EASIIAGLVK APSHYSPTAD AKAAVERAQV VLETMQDAGA ITPAQASNAD LKNIKLAEEA
GQNSARYFTD WVLPQLDQVL PDNDQPIEVW TTLDPAAQHA ATEAIQGNVP NGAQGALVSV
DRDGAVLAMV GGTDYVTSNY NRATNAVRQP GSAWKLFVYL TALEAGYKPD DKVVDEPVTI
NGWSPRNSGG KYAGQIDVRT AFAYSKNTVA AQLGNEVGFG AVANMARRFG ITTPINTMPS
MVLGSSEVRM IDMVRAFAEV QAKGTSVTPY GIRKVTTTDG EVLYSHRDET PQQLVPDYVA
AGITDLLQTA VSIGTGRAAQ IGRPVAGKTG TTSSNKDGWF LGFSSGITTG VWMGRDDAKP
VPGLQGGTAP ARAFAAYMRS ATAKRPPEKF QTELKLPQYQ IEPDDEVLQN NPDNYFYVDP
NGNIVNHQGQ PTDAAQGTDG TTRAAPTQGR DDTVPVPDDQ GAAASDDFLD RATGRQGSAT
AAARRTPSTT PHATATPRAS ARTGTTSANT Y
//