ID A0A1F7JCF7_9BACT Unreviewed; 743 AA.
AC A0A1F7JCF7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-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=A3H78_03245 {ECO:0000313|EMBL:OGK53294.1};
OS Candidatus Roizmanbacteria bacterium RIFCSPLOWO2_02_FULL_36_11.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1802071 {ECO:0000313|EMBL:OGK53294.1, ECO:0000313|Proteomes:UP000177418};
RN [1] {ECO:0000313|EMBL:OGK53294.1, ECO:0000313|Proteomes:UP000177418}
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:OGK53294.1}.
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DR EMBL; MGAV01000021; OGK53294.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7JCF7; -.
DR Proteomes; UP000177418; 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 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 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 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 135..310
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 398..675
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 743 AA; 83447 MW; 2B932DB21C656213 CRC64;
MAKSTAKFNN LDYIIKVFIY QILLFFINFL IFTGDLIILS IRYILRLVII LPINQLKKLI
LKLSRKVKQI FSLVIKPKLP LIDFFKIKYF VIGFLIAFIF ILLFIGIGFI KSLPDPKLIG
KVNFAVSTQI LDRKGRLLYE VYGNENRIPI KIDTLPKYVI SATIAIEDKD FYKHNGVSIW
GGILRALKDS IIKKDLQGGS TITQQLVKAS LLTPERTIQR KIKEMIIALQ VEKIYSKSQI
MEMYLNQVPY GGTAYGIQQA AKVYFDKNAK DLTLSEIAYL AGLPKAPSIY SYYANPEYAK
SRRNEVLTKM LQLKFITRSE FDRESPLPLK IVPLKQLIRA PHFVFYVKNI LEQKYGIRSV
ETRGFRVRTS LDLDIQDEAE LILSEELKKI ENLKVNNGAI LITHPSTGEV LAMVGSKNYY
EDGVGAFNVT TSQRQPGSSI KPLMYSLALT KGFTAVSMVD DSPIIFKIPG SKPYRPINYD
GTFHGLITLR SALANSYNVP AVKMLNTLGV KNFIYHARQM GITTWEDESR YGLSLTLGGG
EVKMTDMAVA YGVFANSGNK VNLNPILDIY DYQGYPIEVN TKVDRTHVLD EGVSYIIYDI
LSDAKARLAA FGNNSPLNIQ QFKVAVKTGT TNEKKDNWTI GFTPKFLAAV WVGNNDNTPM
NPLLTSGITG AAPIWSRVMA SLLSKSISSE FDENPLATNT YQIPTNIVEK KCGGIAEYFV
KGTEKAPCQP EFLSPTPTTI QQQ
//
