ID A0A1N6P5F9_9BACI Unreviewed; 899 AA.
AC A0A1N6P5F9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN05443094_101392 {ECO:0000313|EMBL:SIP99496.1};
OS Domibacillus enclensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=1017273 {ECO:0000313|EMBL:SIP99496.1, ECO:0000313|Proteomes:UP000186385};
RN [1] {ECO:0000313|EMBL:SIP99496.1, ECO:0000313|Proteomes:UP000186385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIO-1016 {ECO:0000313|EMBL:SIP99496.1,
RC ECO:0000313|Proteomes:UP000186385};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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};
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DR EMBL; FTLX01000001; SIP99496.1; -; Genomic_DNA.
DR RefSeq; WP_045852464.1; NZ_MWSK01000001.1.
DR AlphaFoldDB; A0A1N6P5F9; -.
DR STRING; 1017273.SAMN05443094_101392; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000186385; Unassembled WGS sequence.
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 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:SF29; PENICILLIN-BINDING PROTEIN 1A; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 90..264
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 359..641
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..34
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..719
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..845
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 97359 MW; 0CF490AF544617E1 CRC64;
MSDEYKSRTE KRSQQKKKPA RSPKKTKTKK APASKKRSIV KRIILGAFLV ALLVLIGGAG
LFAYYVKDTP EIDEAMLKDP ISSKINADDG SLLTNIGSER REYVEYDDIP VLVRDAFIAT
EDSRFFEHKG IDPIRLGAAV MKNVTDGFGS QGASTITQQV VKLSFLSSDK TLKRKAQEAY
LAYKLEQEYS KEEIFEMYVN KIYMSGPING VKAAADYYFG KELSELSLPE AAYLAGMPQS
PNNYNAFTNP ENAEKRKDVV LSLMNQHDKI SAAEMEEAQD QNITDFLLDE PVSKSGVDPE
YDAFVDLVIE EVEAMGYNAY TDGLTIETTL DKEAQEYMYQ LLNSDEYVNY PSDLFQAGIA
LTDTQTGAIR ALGGGRNQEV QRGLNYATDI KRQPGSTIKP ILDYGPAIEY LKWSTYEQIE
DSPLQYSGGG SVGNAGGSYA GMMSMRDALA RSKNTAAVRT FQEVGFEDAY EFAGKLGINL
ENEYESYGIG AMDGDEGISP LQMAGAYSAF GNGGIYNEPH TVTKVTLADG TVVENDITSE
PAMSDYTAYM VTDMLKSVVD YGTGTAANIP SLHMAGKTGT TNYTDDELQK YDFPSSASPD
AWFVGYTTNY TAAIWTGYES RTEYLSKESQ QIAKELFKQL MTEVSEGVDT PDFEKPDSVL
ELPIVKGSNP AVVAGSGVSD SNKTYELFIR GEQPKRTTPV EEPEEDEEEE QEEEQPEEET
ASGSITGLSA SADASGNMSV SWGYSGDGSP TFSVSNGQET QSIGGFSTVF GGGQPGETYS
ITVTATVDGE SIDSASTSVT IPGGEPAEPE EPEPEPEPEP TPEPAEPEPE PEPEPEPEPE
PAPEPEEPQT EQPANGNSGN NGGNDDATGN SSGNIENGNG STQSNGSQDT EPTEEAPAE
//
