ID A0A1Q7IG66_9CHLR Unreviewed; 948 AA.
AC A0A1Q7IG66;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=AUH89_00985 {ECO:0000313|EMBL:OLC62649.1};
OS Ktedonobacter sp. 13_1_40CM_4_52_4.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805230 {ECO:0000313|EMBL:OLC62649.1, ECO:0000313|Proteomes:UP000186693};
RN [1] {ECO:0000313|EMBL:OLC62649.1, ECO:0000313|Proteomes:UP000186693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(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:OLC62649.1}.
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DR EMBL; MNFP01000019; OLC62649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7IG66; -.
DR Proteomes; UP000186693; 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:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
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 PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF11; PENICILLIN-BINDING PROTEIN 1B; 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 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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 172..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 243..452
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 566..846
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 38..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 948 AA; 104415 MW; C7F69326A71B33EB CRC64;
MYDVPMSNDF WNQQYLNGHK PIEINGAARS VSILRDYRQQ PQQGQEVQQY APLSTPPPQG
YSPYTPPPAP GQMYNNGEQQ GWPAPQSWPS ANNGQQQEQS WVANTLQKVR RWSGRIAAVP
PVDPNPLVLY RPGKSWEQER PKTKPWKRSR TVRVAMLMKH RRVRWRQRRP KAGVIASGIL
IALLLLLLIS ASASSAYAYK YYQDQLPRLQ GLANQQISQT SRIYDRNGTL LYEAYDNSHI
GGGRRTPVSY NFLPQILKDA QISAEDPTFW TNPGIDPQAI LRASGQYLHA GAVVSGASTI
TQQVIKNLTN NAAQTINRKI SEAALAIGLT QQYPKEKILE MYFNISPYGA QNLGVEAAVE
DYFHISSQCD KNFNCTPGVY YLNCDAAHVQ QCHPEQCSQS NYCDPLLGLA RASLLAGMPQ
SPAIYDPTFG LIDAATGQKY YLERQQYVLS QMLRWNVNVP GLGPITQDKV NQAEALTAKT
QFPPYTHPYY HGCQHFVNWV IEQLTAQLGD AFFTGGFNIY TTIDYRLEAY VERAIKRHLQ
KPELQLFPVA RVGVLSSPDY NVYDAAAVVM NAKTGEVLAM AGSANYNSKS SKIDGQFNSA
VHALRQPGSS IKPIVYTTAF QQGWYPGMVI PDHKTYFPHG ISGSPAVCVG PTGAYCPQDY
GGGYSNSNTN IRIATADSRN IPAIKASIYA GVGNVINMAQ RFGITAVSQN RDNNTSFALG
TSGIPLIQMV GAYQVFADNG VRVPPRSILD IWDNYGHHLY HFDPAHPGGI QVISPQIAFL
MTSVLSDEYA RRIEFWPDHD LSFWGNVNYP NPGYPNVAAK TGTTEDFKDN WTLGYTTRVV
VGVWAGNADD SAMYNVAGIT GAAPIWHSVM TYVSGMCNSA NDGIPCPNTN LIFKPHTFTP
PPGVVQACVS SSNGLAGNGN CDWMLDGEQP KSAGMVNPSN KPTPAPTP
//