ID B8EDE4_SHEB2 Unreviewed; 1025 AA.
AC B8EDE4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=Sbal223_1517 {ECO:0000313|EMBL:ACK46022.1};
OS Shewanella baltica (strain OS223).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=407976 {ECO:0000313|EMBL:ACK46022.1, ECO:0000313|Proteomes:UP000002507};
RN [1] {ECO:0000313|Proteomes:UP000002507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS223 {ECO:0000313|Proteomes:UP000002507};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J., Konstantinidis K.,
RA Tiedje J.;
RT "Complete sequence of chromosome of Shewanella baltica OS223.";
RL Submitted (DEC-2008) 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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; CP001252; ACK46022.1; -; Genomic_DNA.
DR RefSeq; WP_006082332.1; NC_011663.1.
DR AlphaFoldDB; B8EDE4; -.
DR KEGG; sbp:Sbal223_1517; -.
DR HOGENOM; CLU_012369_0_0_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002507; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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 PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF00912; Transgly; 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:ARBA00022670};
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 38..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 158..348
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1025 AA; 116747 MW; 3D762D0FF1CEC6C6 CRC64;
MPNSPSEMKF ENYRPRPPQP EPKVKVKTPR KARSKGRVWF LFFILICCIA LLIGLEVKTS
FYQAKYINQY AKTLTYELEN SPSTAVIYPS YGPFDERHGY SKLPQYIDRL MQRNFQVTQQ
VAFSPALQEY AQLGFFPPYH EKAQSGLTLL DCRNTDLYEF AYPKRVYQDD DKIPNEIVNT
LLFIENRELW TTEDKLNPVI DWPRFVVAGM SQIAEMVGMN VSTAGGSTLA TQIEKFRHSS
QGLTLSIKDK LLQIGSASVR VYQQGENTEP ARKRIVQDYL NTVPLSSAPN HGEVHGIGDG
LWAWFGTDFD TANKLLASPQ IKGNAAKRGQ VFRQVVALMI AQRRPSYYLL QGHEDLENLV
DSHIRLLGQY YLIDRGLRDA ALAQKLQFRV TKPQRNTQSG ADKGVNTVRI RTAGMLNVGL
YDLDRLDLTV NSSLHSDLQQ QVSHYLRSLA QVSTAEQVGL LGERLLEPSQ LQNVLYSFTL
YERTDTANRV RVQTDSTDQP FDINEGSKLE LGSTAKLRVM ATYLEIIAEI HEKYSKKHGI
ELESIIIEPR DHLTRWAIDY LIVNPDRRLD RMLDAALQRE YSASTSEQFF TGGGLHVFNN
FKKSEDVKTP TLYQALQDSI NLPFVRLMRD IVNYSSSMQN EGNMAQLLRN DKDPRRDEYL
RVFADREGNT FVTKFYRKYK KVAANERFGM FFDGLSQSEQ QLTSAYRYLL PDEPMSAFKA
FLQQRLPQVS YTDGRIKSLY NKYGPDKYNL PDQGYIARVH PLELWVLDYL NHNPDANLND
VKQASEAQRQ EVYRWLFRTR HKNARDVRVQ VMLEVEAFLD IHQRWARLGY PFDAMVPSLG
SALGSSGDRP AALAELMGII QNDGYRLPTV RINQLHFAAD TPYEVTLENQ NTQGERVMRH
EVAQALKAAL ANVVQNGTAR RLKGIFTDEK GEMLAIGGKT GTGDNRIVTQ MQQGKKVATT
AMNRTATFVF YLGDKYFGTL TAFVPGSKSD DFSFTSALPL QVMKGMMPIL SPYVKTEQGM
CVVNE
//
