ID A0A1H9IT13_9GAMM Unreviewed; 682 AA.
AC A0A1H9IT13;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN04488038_110166 {ECO:0000313|EMBL:SEQ77720.1};
OS Solimonas aquatica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Solimonas.
OX NCBI_TaxID=489703 {ECO:0000313|EMBL:SEQ77720.1, ECO:0000313|Proteomes:UP000199233};
RN [1] {ECO:0000313|EMBL:SEQ77720.1, ECO:0000313|Proteomes:UP000199233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25927 {ECO:0000313|EMBL:SEQ77720.1,
RC ECO:0000313|Proteomes:UP000199233};
RA de Groot N.N.;
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};
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOFS01000010; SEQ77720.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9IT13; -.
DR STRING; 489703.SAMN04488038_110166; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000199233; Unassembled WGS sequence.
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 PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000199233}.
FT DOMAIN 69..225
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 299..538
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 682 AA; 75466 MW; EB1EF300370BBB76 CRC64;
MKARLLRGVK WGALAALSLL MLATLLSQRA LPERLQPSLQ GAPPQILDRE GQPLHSVYDG
GLNLYEQRAL EAMPLALRQA FVEAEDRRFW RHSGVDWRAR AMALRVNLRA GRALRGASTI
SEQVVRILNP RPRTLWSRWV EGFEAWRLEA RFNKSEILEF YLNQVPYGGN RRGVVQAADY
YFARSLDTLS QDEMLALAVL VRAPSRLARE PQALLKRVQQ LAQRLQLPPP QDLLALQRRS
APLEAAYFLA QLERELATQV PQRASLRSSL DSGLQADTER YLAERLQELS REGAQQAAAL
VVDLDGNRVR AYAAADARAP QAIGIDPLQV PRQPGSTLKP LLYALSLEQG WRADTVIEDA
TLRERVNEGL HEYRNYSRQH YGAVTLAEAL GNSLNIPAVK ALQFVGQERF LSRLQDLGVR
SLRQSAAFYG DGLALGNGEL SLFELVQAYT ALAREGLWQP LSLREDGEAP LPRRLIRPEA
ARAISGILAD ADSRRLEFGD GSLLSFAQRT AVKTGTSSDY RDAWTIAYNG RYLLGIWVGN
LSGRATQGVT GARGPALLAR SLLARLPEAG ALRAAPPPSA LARAAPAAEP QAEDPVLLQP
FEGLLMARDP RIPETLQAFR FELGWRQPLR SVRWELDGEF LAQTADKFLD WPLSAGVHRL
RAVATAASGA SAATPEVSFR VR
//