ID A0A168PRC6_9BACL Unreviewed; 864 AA.
AC A0A168PRC6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=PBAT_08550 {ECO:0000313|EMBL:OAB46997.1};
OS Paenibacillus antarcticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=253703 {ECO:0000313|EMBL:OAB46997.1, ECO:0000313|Proteomes:UP000077355};
RN [1] {ECO:0000313|EMBL:OAB46997.1, ECO:0000313|Proteomes:UP000077355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5836 {ECO:0000313|EMBL:OAB46997.1,
RC ECO:0000313|Proteomes:UP000077355};
RA Shin S.-K., Yi H.;
RT "Draft genome sequence of Paenibacillus antarcticus CECT 5836.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:OAB46997.1}.
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DR EMBL; LVJI01000013; OAB46997.1; -; Genomic_DNA.
DR RefSeq; WP_068648537.1; NZ_LVJI01000013.1.
DR AlphaFoldDB; A0A168PRC6; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000077355; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase 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 Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR036116; FN3_sf.
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 InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF32; PENICILLIN-BINDING PROTEIN 2A; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 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 Reference proteome {ECO:0000313|Proteomes:UP000077355};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..256
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 348..623
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 864 AA; 94462 MW; E0D11797309D27F3 CRC64;
MANNRPTRAN ANTEPPKKKK KKRKLSKKRL FWTLFFTAAV AIFCALAGYL FITVNGERLY
NENKDKMIVA ENSKVYDRNG KLMGQLSIQK SEPVDSDQIP DLLKNAFIAT EDKRFMEHGG
VDIWSIGRAA VKDIIARAKV EGGSTITQQL AKNIFLTREK TFFRKATEVS IAMALENNNT
KDEIITMYLN RINFGGQIYG IKAASQYYFG VNDLNNLKVW QMATLAAMPK GPTKYNPLRN
PENSKERRAI VLQLMQEQGY ITAEERETAK NVVYDYTPPA KKQQYLAFMD YVMSEAEEVT
GLSQDDLNVG GYKIYTTMDA NAQQVIEKEF ADDSNFEKSA DDVQVQASMV IMNNDTGAIV
ALMGGRDYER KGYSRVTSSR RQPGSALKPI ASYAPALESG QYTKDSLLSN KKQCFSNYCP
GNLHGYSDTI SMPDAIQKSE NIPAVWLLNE IGVNTGFKFA EKMGISLDKE DKNLSLALGG
MSKGTNTLEM TQAYSAFANG GTLNEAYSIK QIKDSDDKVK YEHKKDGVEV MSKDTSVQMT
QMMKNVVDSG TGKKAAISRP VAGKTGTTQS GIKGNNSNRD VWFVGYTPEL TAAVWMGYDK
PDKTHLLHKS SSLAATFWGK VMEQAIQGFE AKSFPESETV KPPVEVPVVP DIVDVVTGLS
GAYDPNTQIV SLNWNGVEGN NVQYHVYRKE SSESEFRLIK DAATASNIED FDIVEGFTYE
YYVTAFFADT NTESEKSNFV QVFTEPLEPE IEPEPDVEQP DINNGNGNGN GNGNNGSGNG
NGNGNGNNGN GNNGNTGGGT IPGVPETNPG TGGESIPPDG TTVPPEQVVP PVGEDSGVTS
PEDPGSVNTG TTENNVESQG TTTP
//
