ID A0A170U8P7_9ACTN Unreviewed; 808 AA.
AC A0A170U8P7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=STXM2123_119 {ECO:0000313|EMBL:GAT79417.1};
OS Streptomyces sp. F-3.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1840095 {ECO:0000313|EMBL:GAT79417.1, ECO:0000313|Proteomes:UP000078145};
RN [1] {ECO:0000313|EMBL:GAT79417.1, ECO:0000313|Proteomes:UP000078145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wang L.S., Gao P.J., Liu L., Zhang H.Q., Cheng Z., Sun X.M.;
RT "Streptomyces sp. F-3 geneom sequencing.";
RL Submitted (MAY-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:GAT79417.1}.
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DR EMBL; BDDR01000001; GAT79417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A170U8P7; -.
DR STRING; 1840095.STXM2123_119; -.
DR Proteomes; UP000078145; 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 Reference proteome {ECO:0000313|Proteomes:UP000078145};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 50..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 96..268
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 370..623
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..709
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 808 AA; 85993 MW; 0A8BBF44835B4B1E CRC64;
MHTMSDEPKP QPPHRDEAAP QPAAHADAGA DDRPRRTGWR RAVPTWRMML GGFIVVTLLG
IGAFFLGYSL VRIPPANALA VKQANVYLYA DGTEIARDGE INRENVGLDQ ISKAAQHAIL
AAEDRDFYTE SAVDPKAMLR AAWNTATGKG RQSGSTITQQ YVKNYYLGQE QTLTRKVKEF
FIAIKLDRNQ SKDKILEGYL NTSYFGRNAY GIQAAAQAYY GIKAKDLDPA RAAYLAALVN
APSRYDVVAH PENKPAALAR WNYVLDGMVS EGWLSPAERA RTTFPMPKEA TAPVGMAGQR
GYIVRAVKDY LAKNGILDEE QLDAGGHRIT TTLRKHQQDA FVEAVDDQLM SKLDKKNRKV
DTYVRAGGAA IDPRTGELVA LYGGIDYVKQ YTNNATRRDF QVGSTFKPFV FTAAVEHSSQ
TRDGRLITPN TYYDGTNKRP VEGWSGFYAP ENEDQRSYGT ITVREATDKS VNAVYAQMAV
DVGCEKVKDT ALALGLPADT PSLTATPSIA LGVANASVVD MAQAYATLAN HGKHIPYTMI
KKITRNGNEI IDLPERDESQ KISRQAADTT TAVLRSVVQN GTATAAQAAG RPAAGKTGTA
EEDKAAWFAG YTPDLATVVS VMGQDPVTAH HKPLYGALGL DRVNGGGPPA QIWAQFTRDA
LRGRPVTDFD LQLQPGADQP AAPPTAPAET PDADGEDEHD DTDTGDQDSQ DQDTEGREQD
TEGRGTEGTT GTTTEGTTGD TGGLPPTGGT GADTGGTPPG DTAGTPGGSG GPGDPGGPGG
HDGGWGSPGG TTGDGTTTTG VFGGRRPS
//
