ID U4V551_9RHOB Unreviewed; 713 AA.
AC U4V551;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=HIMB11_01767 {ECO:0000313|EMBL:ERL97816.1};
OS Rhodobacteraceae bacterium HIMB11.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1366046 {ECO:0000313|EMBL:ERL97816.1, ECO:0000313|Proteomes:UP000016848};
RN [1] {ECO:0000313|EMBL:ERL97816.1, ECO:0000313|Proteomes:UP000016848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB11 {ECO:0000313|EMBL:ERL97816.1,
RC ECO:0000313|Proteomes:UP000016848};
RA Durham B.P., DeLong E.F., Rappe M.S.;
RT "Draft genome sequence of marine alphaproteobacterial strain HIMB11, the
RT first cultivated representative of a unique lineage within the Roseobacter
RT clade possessing a remarkably small genome.";
RL Submitted (AUG-2013) 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}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000256|ARBA:ARBA00007090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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:ERL97816.1}.
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DR EMBL; AVDB01000005; ERL97816.1; -; Genomic_DNA.
DR AlphaFoldDB; U4V551; -.
DR STRING; 1366046.HIMB11_01767; -.
DR PATRIC; fig|1366046.3.peg.1795; -.
DR eggNOG; COG0744; Bacteria.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000016848; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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 InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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 3: Inferred from homology;
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:UP000016848};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 123..305
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 393..631
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..37
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 713 AA; 77546 MW; 0D6C2794820C5519 CRC64;
MTNKGKKPRL VAENRYPKTG AAKRSAKKKT ATKRKKTPIA KKRGNLFTRF ISGLIRFVVT
VLWRVFWRGT LAIAIMLAIG IGYYMQDLKP YEELLDGRAK GSVTLLDRSG AVFAWRGEQF
GGIITANTVS PHLKNAIIAT EDRRFYQHFG ISPRGLASAI RINLREGRGP LSGHGGSTLT
QQTAKLLCMG TEFDPKKWKN ERAYERECQE GSLWRKVKEA TFALALELKY TKDEILTIYL
ARAYLGAGAR GFEAASHRYF GKSASEVTVS EAAMLAGLLV APSRYAPTNN LKRSQERANL
IIGLMEAQGY ISSTSAQLAR INPAQLSDAA AAQAGGYFAD WVMQEAPDFL TRTTTEDVII
QTTLDQSMQA KAEEALKWVF DNKVSPESKA QAAIVVMSAD GAVRAMVGGR QTKVAGAFNR
ATQALRQTGS AFKPFVYASA LDLGYSPMDK VVDEPITLNI PGSGPWSPKN YTKEFYGTVT
LNEALRQSLN IPAVRISEAV GRDNVRRVAS NFGISTDLAQ GPAIALGASE STLIEMTGAY
AGILNQGLAV TPHGITDLRL SGEISLFSGG SKRVGEQVIL KQTAQDLIFM MENVVRTGTG
QRARFGDWEI AGKTGTTQGA RDAWFIGFTA DYVAGVWMGY DDNTPLTGVT GGGLPTEIWR
ETMQRIHEGI TPKPLPMSRN IAATGQSSLP IQGSRGDESN VIDRLLRGIF GLN
//
