GenomeNet

Database: UniProt
Entry: F1Z4Z7_9SPHN
LinkDB: F1Z4Z7_9SPHN
Original site: F1Z4Z7_9SPHN 
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}.
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; 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
//
DBGET integrated database retrieval system