ID A0A1L3ZZL3_9SPHN Unreviewed; 991 AA.
AC A0A1L3ZZL3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=BSL82_09140 {ECO:0000313|EMBL:API61055.1};
OS Tardibacter chloracetimidivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Tardibacter.
OX NCBI_TaxID=1921510 {ECO:0000313|EMBL:API61055.1, ECO:0000313|Proteomes:UP000182063};
RN [1] {ECO:0000313|Proteomes:UP000182063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JJ-A5 {ECO:0000313|Proteomes:UP000182063};
RA Lee H., Ka J.-O.;
RT "Complete Genome Sequence of alachlor-degrading Sphingomonas sp. strain JJ-
RT A5.";
RL Submitted (NOV-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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; CP018221; API61055.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L3ZZL3; -.
DR STRING; 1921510.BSL82_09140; -.
DR KEGG; sphj:BSL82_09140; -.
DR Proteomes; UP000182063; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
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 PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF00912; Transgly; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000182063}.
FT DOMAIN 130..278
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
SQ SEQUENCE 991 AA; 109220 MW; F30EBD8959548EA9 CRC64;
MARWRPAIIW TAAAGVLALA TYGEMHYSLL QSAVFSSLAR TMDSSVRRGS DPDTGFPEHG
PYDSRLGYVA LPHYLGALEQ RGYHITAQAR QSPAMATFRK IGGFPPYEEK STAGLTLRDA
NGRLYYAARH PSAVYPDFNA VPPLVVNALL FIENRELLNP DTPRRNPAVE WDRLGRAVLG
YATGGLLMPS GPGGSTIATQ LEKMRHSPGG RTGTPVEKLR QMVSASMHAY RDGPDTMDER
RQLVVDVLNS TPLAGRVGHG EVIGLGEGLA LWFGADFNRA NGLLRKAGDG DANLPEAGAA
FRQVLALLIA QRRPSFYLRG GRAELEALTA SYLRLMANAG VISMRLRDAA LRAPLRFADG
APPPRRLPPS SVKAVNGTRF ELMRMLREPS LYTLDRLDLT ADSSLDASVQ AEVTALLRSL
DDPEQLKALG MTGGRLMNGD PAKVAYSFTL FERGTGANHP RIQTDSVDRP LDINVGTKLE
LGSTAKVRTL ITYLDIIARL YEEQRRLGPA ALARTAETGD PLSRWVAAHL IEHGDPGMAG
MMQAAMERKY SASTGERFFT AGGTHRFANF GRHGGYIPVD KALQQSVNLV FIRMMRDIVD
HEIARITARK GDMIADVNHP QRMVYLRRFA DMEGQQFLRQ FHRDYRGLAP PAILERVAER
ARYLRPRLAA AYRTVLPSIT EPEFARLIDR FATEKPADAA AMRKLYDTYA PDRLSLADRA
YVSGIHPLEL WLAGHLYRHP GASMREIVAA SADVRQESYG WLFKSSRIAA QNRRIRTLLE
QEAFVPIHAQ WKRMGYPFDR LVPSYATAIG TSGDRPDALA ELMGIIVNHG VRLPTVRIER
LRFAANTPYE TIVEADPPEP VRVLRPEIAA VVRRALVDTV ESGTARRASD SFHDASGAAM
VVGGKTGTGD NRTDRYARGG RVIGSVTRSR TATFVFFIGD RWYGTVTAHV EGADAAQYRF
TSALPTQLFK SLTPILEPLV QRPPTPARGR S
//