ID K6WTL1_9MICO Unreviewed; 733 AA.
AC K6WTL1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE Flags: Fragment;
GN ORFNames=KILIM_019_00860 {ECO:0000313|EMBL:GAB95432.1};
OS Kineosphaera limosa NBRC 100340.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Kineosphaera.
OX NCBI_TaxID=1184609 {ECO:0000313|EMBL:GAB95432.1, ECO:0000313|Proteomes:UP000008366};
RN [1] {ECO:0000313|EMBL:GAB95432.1, ECO:0000313|Proteomes:UP000008366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100340 {ECO:0000313|EMBL:GAB95432.1,
RC ECO:0000313|Proteomes:UP000008366};
RA Yoshida I., Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y.,
RA Ohji S., Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Kineosphaera limosa NBRC 100340.";
RL Submitted (AUG-2012) 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:GAB95432.1}.
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DR EMBL; BAHD01000019; GAB95432.1; -; Genomic_DNA.
DR RefSeq; WP_006591964.1; NZ_BAHD01000019.1.
DR AlphaFoldDB; K6WTL1; -.
DR STRING; 1184609.KILIM_019_00860; -.
DR eggNOG; COG0744; Bacteria.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000008366; Unassembled WGS sequence.
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000008366}.
FT DOMAIN 52..226
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 325..572
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 622..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 733
FT /evidence="ECO:0000313|EMBL:GAB95432.1"
SQ SEQUENCE 733 AA; 75883 MW; 35AA3A1AA02027D6 CRC64;
MTPKGILAII GALFALGVLL VLAAFALVRV PDPNEAARAQ TSIIYFADGQ TEMHRFAEVN
RESIPLSQVP KHVQEAMLAA EDRSFYENPG FSPTGIARAV WATVTGGPTQ GGSTITQQYV
KNYFLDQDQT VTRKARELII SIKIEQQQSK DQILENYLNT IYYGRGASGI EAAARAYFNK
GAADLTVGEG ALLASVIRGP SLYDPALGAK QEQNARDRVD YVLAGMVEQG WLTAAERAQV
DFPEVAPPRQ NAAPSGPNGY LVAMVKNELT QKIGLSEAEV DRGGLRITTT IAKQAQTDAI
TAVENNRPSG GRGDDVRVGL ASIKPGDGAI LAIYGGSDFR SQPYNSATQA QLQAGSTFKP
FTLVAALEKG ISTRTQLDGS SPAYFPEFRG GGNANGRVTN FGNASYGQVT LREATAKSIN
TAYAELNIDV GPQATKNVAV RMGLPENTAG LDDNYANVFG TASPRVIDMA NAYATLAAQG
KRAEPYIVQS VTSVDGTYAG WTASPQLTDA ISPQVAADAV DAMTRVVREG TAVGASRLGR
PAAGKTGTTT DNLAVWFDGF TPQAATAVAL YMPDEQGNAQ PLRGIGGRSE LTGGTYPVQI
WTAFMRELLS GQSVEDFPAR AGVGDSEVRW VPPPAPSPTA TATQTPTQTQ TPTDTPTPTD
TWSPTDVPTT PEPGDGDNGS PQPPGDGGDN GTGGGGGGGG RGGGGDGGGG GGGDDGGGEA
ANSGGQGGQG GTG
//
