ID A0A1F3QT27_9BACT Unreviewed; 569 AA.
AC A0A1F3QT27;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE Flags: Fragment;
GN ORFNames=A3K10_00335 {ECO:0000313|EMBL:OFY93069.1};
OS Bacteroidetes bacterium RIFCSPLOWO2_12_FULL_31_6.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797363 {ECO:0000313|EMBL:OFY93069.1, ECO:0000313|Proteomes:UP000176519};
RN [1] {ECO:0000313|EMBL:OFY93069.1, ECO:0000313|Proteomes:UP000176519}
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:OFY93069.1}.
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DR EMBL; MEPA01000489; OFY93069.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3QT27; -.
DR Proteomes; UP000176519; 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:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
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; IPR011815; PBP_1c.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 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..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 49..224
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 304..522
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT NON_TER 569
FT /evidence="ECO:0000313|EMBL:OFY93069.1"
SQ SEQUENCE 569 AA; 64891 MW; 7CAF09A48FAD43E5 CRC64;
MKQLNLKQKN IAALLISLIS LFILFIIFDY FFPIKTNINY SSIVVSNDGT IIHSFLNNKD
KWRMKTELDE ISPVLKKTII YKEDKYFYYH PGINLIAITR AIFNNVVKYK RTSGASTITM
QVARMLQPKK RNYVNKFFEM FRALQLEWHF SKEEILQFYL NLVPYGGNIE GVKSASMLYF
QKKPEALSLA QVTTLSIIPN RPTSLRLGEN NTYVVQERNK WLNRFLKEKL FSKQEIEDAL
NEPLDAHRHI APNFAPHFSI RMNYKYPHDA IIKTTLDLRK QQKIEALVKN YITTLKNMNI
SNASVLVINN HTRSVEAYIG SADFNDVDAQ GQVDGVNAVR SPGSTLKPLL YAMAIDKGLI
TSKTIITDVP VNFSGYRPEN YDQQYRGKVS IEKALAISLN IPAVKILDEV GVTQIAEKLS
KANFKWIDKH KSDIGLSLVL GGCGVTLEEM TNLFSCFANY GKYQNLKWIQ DNSDSANFNL
FTPSSSHIVT NILTELIRPD LPYKFENSMH LPRVAWKTGT SYGRRDGWSI GYNVDYTVGV
WIGNFNGEGV PELNGAEFAT PLLFDVFNN
//
