ID   A0A1H7N0U5_9LACT        Unreviewed;       936 AA.
AC   A0A1H7N0U5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-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=SAMN04488099_11338 {ECO:0000313|EMBL:SEL16951.1};
OS   Alkalibacterium pelagium.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Alkalibacterium.
OX   NCBI_TaxID=426702 {ECO:0000313|EMBL:SEL16951.1, ECO:0000313|Proteomes:UP000199081};
RN   [1] {ECO:0000313|Proteomes:UP000199081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19183 {ECO:0000313|Proteomes:UP000199081};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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};
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DR   EMBL; FNZU01000013; SEL16951.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7N0U5; -.
DR   STRING; 426702.SAMN04488099_11338; -.
DR   Proteomes; UP000199081; 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; 3.40.50.12800; -; 1.
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:UP000199081};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        37..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          94..281
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          421..663
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          793..936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        797..854
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        855..919
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        920..936
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   936 AA;  103173 MW;  B05EEFC45C92026D CRC64;
     MKRSEEKKQR QTEETNEPSR FENVVYYFDI FYRVVKALVI MLVVILLVGG SLGAGAAVGY
     FVSLVNGNDI PDHEVMVQQI YDYNETSTMY YAGGEVISDL RADLMRTPVE LEQMSPLLVD
     AIIATEDEYF FDHEGIVPKA VARALVQDLT ESGASTGGST LTQQLIKQQI IGGEVSHERK
     ANEILLAMRI ENYMDKEEIL EAYLNVSPFG RNNKGQNIAG VEEAAQGIFG VPASEVTLPQ
     AAFIAGLPQR PNIFSPYTNT GAIKEDQELG LRRQREVLFR MHREGLITYD EYQEAVEYDL
     TQDFLNSEEI DYEDLSYVYD RGEFEARRIL VIQALERDGI TNEDLEENPD LLGEYEEQIR
     SEIRNGGYQI HTTIDRDVHH AMEETVREYQ DQLGAEQTYT WEDNDGNTQS TTLPVQYGGS
     LIDNETGRII GFIGGRDYEL SQFNNAFQMR RTPGSAIKPL AVYGPAIDAN LLTPATIIPD
     TEVEIRNDWN PATGEWNYYT PTNVGATTNE WITARESLED SKNIAAFKVH AELLEEEVDL
     AGYIRRMGIT EEDVPTETVN LPSFSIGGTD GPSPVGLTSA FSTIGNNGQH ADAYLIERIE
     NSAGEVIYEH EVEQTEVWSP ASNYVLADML RGVHTDGTAE GTIDQLNFSS DWVSKTGTTQ
     DRNDVWYIGS TPRVSFGTWM GYGTNELSLR DDFGLHPSRR NRDMWARIMN AVHAVNPDIL
     GVGENHARPD GVTEDSVIVD TGMKAGEVEA PDGSTFNYSG NTHTELFKSD NVPGTTVYDF
     AIGATDEELE EFWGRASSSD DDDEEDDEDD DEEEETEDDA DDDDQSNDDE ASEAPEPEPE
     PEPEDDDDEE DESSNGNGNG SSNGNNGSDN GNGSSDDTDE SNGNGSSNGN GNGNGNGNGN
     GNGSSNGNGN GNGNSEATPP SDENDDDDND TDDEED
//