ID A9KVQ5_SHEB9 Unreviewed; 1025 AA.
AC A9KVQ5;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=Sbal195_2989 {ECO:0000313|EMBL:ABX50154.1};
OS Shewanella baltica (strain OS195).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=399599 {ECO:0000313|EMBL:ABX50154.1, ECO:0000313|Proteomes:UP000000770};
RN [1] {ECO:0000313|EMBL:ABX50154.1, ECO:0000313|Proteomes:UP000000770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS195 {ECO:0000313|EMBL:ABX50154.1,
RC ECO:0000313|Proteomes:UP000000770};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS195.";
RL Submitted (NOV-2007) 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; CP000891; ABX50154.1; -; Genomic_DNA.
DR RefSeq; WP_006085540.1; NC_009997.1.
DR AlphaFoldDB; A9KVQ5; -.
DR GeneID; 11773071; -.
DR KEGG; sbn:Sbal195_2989; -.
DR HOGENOM; CLU_012369_0_0_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000770; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
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; 116657 MW; 91093F5A6A9F37FD 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 SKPQRNTQSG 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
FLQQRLPLVS YTDGRIKSLY NKYGPDKYNL PDQGYIARVH PLELWVLDYL NHNPDANLND
VKQASEAQRQ EVYRWLFRTR HKNARDVRVQ VMLEVEAFLD IHQRWARLGY PFDAMVPSLG
SALGSSGDRP AALAELMGII QNDGYRLPTV RINQLHFAAD TPYEVTLENQ NTQGERVMRH
EVAQALKAAL ANVVQNGTAR RLKGIFTDES GSPLAIGGKT GTGDNRIVTQ MQQGRRVATT
AMNRTATFVF YLGDKYFGTL TAFVPGSKSD DFSFTSALPL QVMKGMMPIL SPYVKTEQGM
CVVNE
//
