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Database: UniProt
Entry: A0A097EL32_9SPHN
LinkDB: A0A097EL32_9SPHN
Original site: A0A097EL32_9SPHN 
ID   A0A097EL32_9SPHN        Unreviewed;       684 AA.
AC   A0A097EL32;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=MC45_14680 {ECO:0000313|EMBL:AIT08278.1};
OS   Sphingomonas taxi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1549858 {ECO:0000313|EMBL:AIT08278.1, ECO:0000313|Proteomes:UP000033200};
RN   [1] {ECO:0000313|EMBL:AIT08278.1, ECO:0000313|Proteomes:UP000033200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55669 {ECO:0000313|EMBL:AIT08278.1,
RC   ECO:0000313|Proteomes:UP000033200};
RA   Zhou Y., Ma T., Liu T.;
RT   "Using Illumina technology Improving SMRT sequencing Genome Assembly by
RT   RASTools.";
RL   Submitted (SEP-2014) 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   -!- 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}.
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DR   EMBL; CP009571; AIT08278.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A097EL32; -.
DR   STRING; 1549858.MC45_14680; -.
DR   KEGG; stax:MC45_14680; -.
DR   eggNOG; COG0744; Bacteria.
DR   HOGENOM; CLU_006354_2_7_5; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000033200; Chromosome.
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; 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   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:UP000033200}.
FT   DOMAIN          48..214
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          300..521
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          583..684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..624
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        633..669
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   684 AA;  74263 MW;  803821280C250239 CRC64;
     MLAFGALAIA VYVARSQLPS FEELKSSPNG QMIRVHAADG SVIVSMGPSY GEWLSYDSIP
     RVMREATVAV EDRRFYSHPG VDPLGIARSV LIRYERGRWI QGGSTITQQL ARNVFLNNQK
     KFGRKFREWI LALALERKFS KDQVLELYLN KVYYGGGAYG IDAASRKFFG HGANTLNLAE
     AAVIAGLVKA PSNYSPTADA QAAVGRAGVV LDAMVRHGSI TREQASEADP QALRLAPEPR
     QNSARYFTDW ALPQLDTLID ETQAPLDVWT TLDLGMQRDA DAAVRANAPD GAQGALVSLD
     RDGAVKAMVG GKDYVSSIYN RATQAQRQPG SAFKLFVYLA ALEAGHKPED SIVDEPVTIN
     GWSPRNDSRR NSGPVTLRTA FAFSLNTVAA KLGQEVGFTT IADMARRFGI TTPINTHPAM
     VLGTSDVRLI DMTRAFASVA AKGVAVTPYG ITRVTANGQT IYTHEVDRSH VLVAPYVAAE
     MTDLLQTAVN TGTGRAAQIG RPVAGKTGTT TSLKDGWFLG FSSGLTTGVW MGRDDARPIA
     GLHGGTAPAR AFAAFMKPAT ANRPIEQFET QVTLPEWQLE PDEETYFGQP DNGGAMVDED
     GNPVAQAPRD EQQQDEQAIR PQDSAPQQLD DLIDRVTGRD APQPRDDRRD PAAPVRQPLR
     DDRRDGAPAN RQPPRPLQDD RPTQ
//
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