ID W9FNF6_STRFL Unreviewed; 783 AA.
AC W9FNF6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SSIG_02412 {ECO:0000313|EMBL:EWS91939.1};
OS Streptomyces filamentosus NRRL 11379.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=457430 {ECO:0000313|EMBL:EWS91939.1, ECO:0000313|Proteomes:UP000027349};
RN [1] {ECO:0000313|EMBL:EWS91939.1, ECO:0000313|Proteomes:UP000027349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 11379 {ECO:0000313|EMBL:EWS91939.1,
RC ECO:0000313|Proteomes:UP000027349};
RG The Broad Institute Genome Sequencing Platform;
RA Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Godfrey P., Alvarado L., Kodira C.D., Straight P.,
RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T.,
RA Lander E., Galagan J., Nusbaum C., Birren B.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EWS91939.1, ECO:0000313|Proteomes:UP000027349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 11379 {ECO:0000313|EMBL:EWS91939.1,
RC ECO:0000313|Proteomes:UP000027349};
RA Ward D., Fischbach M., Godfrey P., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D.I., Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D.,
RA Pearson M., Richards J., Roberts A., Saif S., Shea T.D., Shenoy N.,
RA Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C., Haas B.,
RA Henn M.R., Nusbaum C., Birren B.;
RT "The genome sequence of Streptomyces roseosporus strain NRRL 11379.";
RL Submitted (MAR-2010) 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:EWS91939.1}.
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DR EMBL; ABYX02000001; EWS91939.1; -; Genomic_DNA.
DR AlphaFoldDB; W9FNF6; -.
DR Proteomes; UP000027349; 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 PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF34; 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 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 80..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 124..299
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 403..658
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 82357 MW; 563986F6ED7044E5 CRC64;
MGELTTSQEP PTDMSDEPQS WAPRDSSGAG ASSGNHRPTA SGEQPGTNPG KPGKPGKPGK
KARPRRTGWR RAIPTWRMTL GTLLGLVVLL GAGVFAAYRL VDIPAANASA TAQSNVYLYS
DGSVIARDGD VNREKVKLSQ VPPTVQHAVL AAEDRDFYSD DRAVDVKAML RAGWNTVTGK
GKQGGSTITQ QYVKNYYLGQ ERTVLRKAKE AIIAVKLNRE ETKDQIFEGY LNTSYFGRNA
YGIQAAAQAY YGKNVEELTT AEGAYLASLL NAPSAYDVVA HPDNRPAAQR RWNYVLGGMV
KERWLTAAER ATTRFPTPGE AKPSNGLSGQ RGYIVQAVED YLNRRGILDA KTLATGGYRI
TTTLDKAKQD AFVKAVADNV TAKTSSNRAA DRNVRVGGAS IVPETGKVVA LYGGIDYTKQ
YVSNATRRDY QVGSVFKPFV LTSAVVNDST TQDGRRITPN TVYDGTNKRT VVGVQGSTDY
APANEDDVDY GDITVRIATD KSVNSVYAQM AQDVGPAKVR ETAIALGIPA DTPDLTAAPS
IALGTANASV LDMAEAYATL ADHGRHGRYV LVEKVTKDGA EIELPERTTE QAVSREAADT
TTAVLRSVVE GGTGTAAQTV GRPAVGKTGT AEEDRAAWFA GYTPDLASVV AVMGQNPDTG
AQTPLYGALG LPRVNGGGVP AETWAAYTEA ALRSSPVQEF DLRTAPGSDE GDELLVDENA
DGGTDPSSSS DPDTSPDTSP DATPGTTPDG SAPPTPGTNT GGTDEGSVSA PDGIGDGDGD
GNG
//