ID W4QNA2_9BACI Unreviewed; 945 AA.
AC W4QNA2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=JCM9152_4406 {ECO:0000313|EMBL:GAE32824.1};
OS Halalkalibacter hemicellulosilyticusJCM 9152.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX NCBI_TaxID=1236971 {ECO:0000313|EMBL:GAE32824.1, ECO:0000313|Proteomes:UP000018895};
RN [1] {ECO:0000313|EMBL:GAE32824.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 9152 {ECO:0000313|EMBL:GAE32824.1};
RA Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequences of Three Alkaliphilic Bacillus Strains, Bacillus
RT wakoensis JCM 9140T, Bacillus akibai JCM 9157T, and Bacillus
RT hemicellulosilyticus JCM 9152T.";
RL Genome Announc. 2:e01258-13(2014).
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:GAE32824.1}.
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DR EMBL; BAUU01000055; GAE32824.1; -; Genomic_DNA.
DR RefSeq; WP_035347381.1; NZ_BAZO01000055.1.
DR AlphaFoldDB; W4QNA2; -.
DR STRING; 1236971.JCM9152_4406; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000018895; 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; 3.90.1310.40; -; 1.
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; 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 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; 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:UP000018895};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..281
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 406..656
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 882..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..906
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 945 AA; 105693 MW; 21DACD484B37B627 CRC64;
MEKENSTFLE KVRGFSKVLH QRTLFRTIGI TYQVFWNLFL IFLVLICMLI FFAGGAAAGY
FVSLVKDEPL LSEDEMRTAV YDYEETSQVF FANDVYLGEL PSDIERHEVS LEDVSEYVIQ
AIIATEDEYF YEHEGIVPKA IMRAMFQEVA NSSLQTGGST LTQQLIKNQI LTNEVSFDRK
ATEILFAMRL ENYLEKDEIL EAYLNIVPFG RNASGRQIAG IQAAAQGIFG VDASELSIPQ
AAYIAGLPQS PFGYTPFRND GSIKDSIDPS INRMSTVLSR MYEAGYITEE ERAEALAYDF
EKSFADFTPS PIEEYPYLTY EVLRRAIDVL SKQQMEEDGV DLSELDQEEQ LEMRQRYQEI
ASRDLRGNGY RIHTTVDKDI YLSMQDSIQN DGLFGPNKGG KPEQVGAVLL ENSTGAIKGF
VGGRTEGSDD HYNRATQAYR PNASTMKPLV AYAPALEIGA VQPGIVIPDT RDHYPDGQEI
RNFDRQHLGL LSVRESVARS RNVPAVRAYR MVPFEQKRQT LLDLGFFLPA DAPYESSTLG
TNDVTVEQNT NAYATFANGG TYVESYMIER IETADGELVY EHEPETREVF TPQTSYLMID
MMRDVLRGVG TASSLPSRLS FSADWAGKTG TSGEDRDSWF VASNPNVTMS VWIGYDDQHV
IEGRSGPKTQ QVWANLANAA YSVDPDLLAP SNRFEAPSGI VSRSICSLTG MLPSTACQEA
GYVTTDLFNA QFLPSEEDGS LESTRYVTIS GKNYIALDST PSEFTEKGIK LSDSFWDIDN
IGQYLPDSMR NIVLGDEAPN NGRIPRDVEN VRINGDELRW SVHSDNDIIG YRVYRATNGT
TNFEPIATIV GNETTTYSIR GNSNSYYVTA IDTAGRESAR STIAEGKDYV PEIIEEEEDE
EEDQEESNRS SNERQNENAN ANSNNNSNNG NRGNNNRNDN DEEED
//
