ID A0A235B5X9_9BACL Unreviewed; 793 AA.
AC A0A235B5X9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=CHM34_09115 {ECO:0000313|EMBL:OYD07631.1};
OS Paludifilum halophilum.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Paludifilum.
OX NCBI_TaxID=1642702 {ECO:0000313|EMBL:OYD07631.1, ECO:0000313|Proteomes:UP000215459};
RN [1] {ECO:0000313|EMBL:OYD07631.1, ECO:0000313|Proteomes:UP000215459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 102817 {ECO:0000313|EMBL:OYD07631.1,
RC ECO:0000313|Proteomes:UP000215459};
RA Belbahri L.;
RT "The genome sequence of Paludifilum halophilum highlights mechanisms for
RT microbial adaptation to high salt environemnts.";
RL Submitted (JUL-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};
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:OYD07631.1}.
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DR EMBL; NOWF01000005; OYD07631.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A235B5X9; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000215459; 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; 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: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:UP000215459};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 93..277
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 405..642
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..793
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 87525 MW; 69B83F1399C1352F CRC64;
MADQKRPSQS NEQKKGPSDT KDPRNKRSRL VRGLLFTSLV LITLFSVGTM ASVGAAAGYV
ASLVNEEPVR PEAKLEEAIT KWSQTSYAYF RDEELIGRMR ADADRKVIQA DNVSPHLVDA
LISTEDREFY EHDGIVPRSI LRAAFQKVTG SEVQTGGSTI TQQLVKQSIL KNNAQTMERK
AKEIFLAQRM ERFFSKEEIL NAYLNSVYFG RGASGRNMLG VQAAAQGMFG VDAKDLNLAQ
SAYIVGMVQR PNAYNPFMGK EALKRGEERM RDVLKNMVEN KKISKDEYKK AAKFDIKGSL
AEKGETNAYQ KYPYITMALE EEAAKILMKE DGLDAKKLSE EGKYRETLNK YRGEVQTGGY
RIHTTLDKDL YEAMNKAAQN DALYAGPITY TVNGRTIKNA KEEVGATLLD TKTGAMLGFV
GGRDFEANNR NHALDARRQP GSTIKPLLDF GPGMDKGVIS PDSVIIDEPL RHSGGVYENY
THRYDGAMTA REALKKSINI PAIKVLRKVG VQRGLDYLRK MNFPVHKNDG EASAIGGFTY
GFDVQRVTAG YASLGNEGKF NEPYMIEKIT DASGETVYKH ESDPVKVYSP QAAYWTTDML
RDVIKSGTGT YVGARVPGYD LAGKTGTTNG TKDVWFMGYT PDITLGVWTG YEYAHRLPND
KRARIVWTKI FQAIDETDPE LASKSSKFKS QPSVGFKCFE CKRAKKEEEK EKKKKKKEKN
QPDQGESPGN GNSGNDDPGN ENPGGGNPGD GNSGNDNPES PGEGDPGDDP PGEGDPDNPD
DGAEIQPTEP DDD
//
