ID A0A1F8PWX7_9CHLR Unreviewed; 957 AA.
AC A0A1F8PWX7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=A2W33_06325 {ECO:0000313|EMBL:OGO27654.1};
OS Chloroflexi bacterium RBG_16_52_11.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797646 {ECO:0000313|EMBL:OGO27654.1, ECO:0000313|Proteomes:UP000179327};
RN [1] {ECO:0000313|EMBL:OGO27654.1, ECO:0000313|Proteomes:UP000179327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGO27654.1}.
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DR EMBL; MGNN01000049; OGO27654.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8PWX7; -.
DR Proteomes; UP000179327; 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: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 Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR013783; Ig-like_fold.
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; PF17957; Big_7; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 146..255
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
SQ SEQUENCE 957 AA; 102614 MW; 54C5CAB76D68EC91 CRC64;
MPSTTQIIRF REQRKARARR YPTRAIGLGC SLLLALLITL SSLALVVFYS NLTAGLPSNE
MLPVLLAPGA GTLLQPTKIY DQTGSHLILA LQNPADVGRQ FLDLESTKPN FFPADLISAT
LSASDPGFWN HPGTILTNTE PETHPSIAQR LINELVLWDE PPGLRRTLRE KLLAMQVTAT
YGREQVLIWF LNSADYGRLV FGADSAARVY FGKPASELNL AEAAILAAVA EAPALNPHDA
PQIAQQRGSE LLNDMLANGV ISPQQAEQAR LAAITFQPSE SLSTNLAPGF SALALSQLSK
VFDLARLERG GYQVITSLDY DLQTQATCAT AALLSSVDSP PGSSETAGGD ECEAARLLQT
QSLSAASNPT ALAANVAILE PATGKILALV GDNKAGLDAL HPAGRSPGTL LTPLIYLSGF
TRGLGPASLL WDIPPTNPTQ VSAGEHFHGP VRLRTALAND YLAAARQVFA QGGSQNLEKV
ARELGLSLDG RVINEDLSAV VNQSRTNLLD ISQVYSVLAN QGVLVGMPSE TDESLRQGTT
LEPIAFLKLT DLTGTTLVEA RGSQVRPVLS PQLSYLLTHI LSDEPARWPS MGHPNPLEIG
RPVAAKLGRT EAGTDAWAVG YTPRLLVGAW VGEKDADSTS EVPVDLAASL WHAVMQYASR
NQPPLGWSFP EGVSNVLVCD PSGLLPSDDC PTVVNELFLA GNEPTHTDTL YRKLQINRET
GRLATIFTPP EQVEERTYLL VPPEAEAWAR QSGIASPPES FDVILSEQTT ADVAITSPSM
FAYVKDSVPI FGEIGTDDLE FYRLQVGKGL NPTAWTQVGE DSSTLAADGV LGVWDTRDAN
GLYAVQLLVV RTDQHVDTAM IHVTVDNQPP EVQILYPSAG QQFDSDTGST ITLRANAEDD
VALHQVDFFI DGKPIATLAQ PPYSTIWRAT AGKHQLSVQA VDKAGNTQTA SLEFTIR
//
