ID A0A2M9ASL6_9BACT Unreviewed; 775 AA.
AC A0A2M9ASL6;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=CLV45_4342 {ECO:0000313|EMBL:PJJ48633.1};
OS Hymenobacter chitinivorans DSM 11115.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1121954 {ECO:0000313|EMBL:PJJ48633.1, ECO:0000313|Proteomes:UP000228535};
RN [1] {ECO:0000313|EMBL:PJJ48633.1, ECO:0000313|Proteomes:UP000228535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11115 {ECO:0000313|EMBL:PJJ48633.1,
RC ECO:0000313|Proteomes:UP000228535};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) 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 -!- 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:PJJ48633.1}.
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DR EMBL; PGFA01000004; PJJ48633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9ASL6; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000228535; 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: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; 2.
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:SF11; PENICILLIN-BINDING PROTEIN 1B; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 81..263
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 437..679
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 775 AA; 87668 MW; 97339163F98C30E3 CRC64;
MAYPATKPKN IRKPQRPGRF TGLTRTLWFL FGGGVLGLIL YILAVSVNFL NLFGRMPNLK
TLENPKSELA SEIYSADGVL MGKYFRENRT PVDYEDLPQN LIDALIATED VRFEGHSGID
FKGLFAIPYY VATGRSRGSS TLTQQLAKVL FRTRGDLNDG TLNDVPGLRM LIIKTKEWIM
AVRLERSYTK REIMRMYLNT NDFGSNAFGI NVAAKTFFNK SPKNLTLEES ALMVGVLNAP
SRYSPVQNPE RAKVRRNWVL YQMRKYNYIT PEEHALAAAK PIVLHYSVEN SNKGIAPYFR
AEVSKALLQW AKETDHDLYA DGLKIYTTVD SRMQKYAESA VAEHMRQQQK LFDAHWKGQL
PWRDENGRII PNFLQTSIKR TERYRSLDNR FDGNKDSINY YLKKKYKMMV FSWKGEKEVL
MSPLDSLAYY KRYLHAGFMA MNPLNGQIKA WVGGTNFKYF KYDHVKQGKR QPGSTFKPIV
YTAAIDQGYS PCYQRPDIAT TFPAVAGRAP YTPKNFEGGF SGRTFTLRQA LARSMNSITA
WLVQKLGPET VVSYAKRLGI TSPIEAVPAV GFGSSDVSIY ELSGAYSTFV NKGVWTAPMM
VTRIEDKNGN VLREFVPQTR EALSEETAYL MTYMLQAATT EQGGTSVILK TGFKFPYEIG
AKTGTTSNYS DAWFMGVTPD LVCGMWVGGE DRSIHFRNGS YGQGARAALP IYGLFMRKVY
ADKSIGVSTS PFPKPEQPLS IEIDCSKYYG GQRDTIPYDQ KLNQTDLQDI DEEDI
//
