ID A0A1F6W7S5_9BACT Unreviewed; 849 AA.
AC A0A1F6W7S5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=A3D42_01845 {ECO:0000313|EMBL:OGI78000.1};
OS Candidatus Nomurabacteria bacterium RIFCSPHIGHO2_02_FULL_41_18.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801754 {ECO:0000313|EMBL:OGI78000.1, ECO:0000313|Proteomes:UP000177777};
RN [1] {ECO:0000313|EMBL:OGI78000.1, ECO:0000313|Proteomes:UP000177777}
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:OGI78000.1}.
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DR EMBL; MFUE01000004; OGI78000.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6W7S5; -.
DR STRING; 1801754.A3D42_01845; -.
DR Proteomes; UP000177777; 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: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 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 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 75..249
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 340..629
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 849 AA; 95847 MW; 365DED41B368B19C CRC64;
MLKIFRRSPK GFQKNKNFWK NITFFTSGVF ILSAGIITIW FSSLQIPDFN TFDERKVINS
TKIYDRTGEI LLYDVNKDIR RTSIDFADMG INIKNATVAV EDSEFYNHSG IRIPSIIRAT
IIAKLTGKKL TGGSTITQQL IKNTLLTAET TMMKKVGRKI KEWVLALKME QVFSKEKILE
LYLNEVPYGG TIYGIEEASR MYFRKKPADL TIAEAAYLAS IPQSPTLLSP YGKNKDKLED
RKNYVLSRMR ELKFISEEEY REAKNEIVVF IPQEFRSIKA PHFVFFIKEY LEEKYGAELV
ERGGLKVITT LDYTLQQKAE EFVREGALEN EKVWDGKNAA LVAIDPKTGQ ILSLVGSRDY
FDKAVDGNYN VATAFRQPGS SFKPFIYATA FSKGFTDKTV LFDLPTEFQT TCDAFGKALP
NHNQEDCYMP DNYDGKFRGP MSLRSALAES INVVAVKLFY LAGLSDSLKT AEEMGISTLT
DINRYGLTLV IGGGEVSLLD MTSAYGVFAN GGIRNTQTGI LMVEDTRGKI LEEYAPSPKE
VLSKNSASIV SDILSDNAAR TPTFGIGSPL HISGREVAVK TGTTNNNKDA WTIGYTPSIA
VGVWAGNNDN QPMKKGGSAV AGPIWNKFMA EALKTLPEEN FEKPDPALYL DKKPILRGFW
QGNENFFMDK ISMMLATPFT PEETKEEKVI TNVHSILYWI DKKNILGPAP ENPESDSQFK
HWEIPVQNWW AQNSYKYEKV TKENKPTGID NVHTPSTEPV IEVLEPNLQK TYRSGEKIQL
KVKSLGVYPL ERMDIFINEV YLGTLNSPFG FSFTPEELDN LRENNELKVI VYDKVFNRAE
NVFYFKVSD
//
