ID A0A090ANR2_9GAMM Unreviewed; 735 AA.
AC A0A090ANR2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=THII_3485 {ECO:0000313|EMBL:BAP57782.1};
OS Thioploca ingrica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thioploca.
OX NCBI_TaxID=40754 {ECO:0000313|EMBL:BAP57782.1, ECO:0000313|Proteomes:UP000031623};
RN [1] {ECO:0000313|EMBL:BAP57782.1, ECO:0000313|Proteomes:UP000031623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kojima H., Ogura Y., Yamamoto N., Togashi T., Mori H., Watanabe T.,
RA Nemoto F., Kurokawa K., Hayashi T., Fukui M.;
RT "Ecophysiology of Thioploca ingrica as revealed by the complete genome
RT sequence supplemented with proteomic evidence.";
RL ISME J. 0:0-0(2014).
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}.
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DR EMBL; AP014633; BAP57782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090ANR2; -.
DR STRING; 40754.THII_3485; -.
DR KEGG; tig:THII_3485; -.
DR HOGENOM; CLU_006354_7_1_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000031623; Chromosome.
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:UP000031623};
KW Transferase {ECO:0000313|EMBL:BAP57782.1}.
FT DOMAIN 62..219
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 310..545
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 735 AA; 83017 MW; 553E97A027E88DF0 CRC64;
MRKFIRVSLV TLLLGFSIVF GKTLLDLAPL PTTLSVTTSP IRKLQVLDRH AIPLIMTYQN
DWNIYDYVPL HEIPELLQRI FLLAEDKRFY EHGGPDWRAR WHALFQNILA LRIVRGASTI
TEQTVRMLYL RPRTFWSHWL QGIEASRLER HFSKADILEF YLNQVPYANQ RRGVVQAARY
YFDRDLDTLN LKEMIALAVL IRAPSRLDLR RNKTEIEAPI VRLAQRLFEL NLISNTDYQE
ILTTPLSLRE ASLPIQATHF VNYIYTSHAA SPLPHLGRLY TTLDAKLQSF VQLILNQRIQ
ELQNQNVSHG AVLVVDHQTN EVLAWVNSGR PSPEISGSQI DAVTIPRQPG SALKPFLYAL
ALEKGWTAAT LIDDAPLAEA VGVGLHDYRN YSRSYYGSLR LRDVLGNSLN IPAIRTIQFV
SAQSFLQRLH QLGISSLTAR SDYYGDGLAL GNGGVTLLEL VQAYTVLAYQ GLFRPLKVLR
NTSPTKAISV FTPEIASIIA DILSDSDARR LEFGRGTLLR FPIQTAVKTG TSTDYRDAWA
VGFNHHYTVG VWLGNLDQQP MSQVSGATGS ALILRAIFAE LNRYEETQPL FLSHKLVKVN
ICRTTGQLAT PTCPSKLEWF IPGSQPVSSD QPELTPVKPL KKAFYLKQPT PDLQLAMDPR
IPDEYEAFAL MLSDTSLKVN SIEWVVDDEV IGTTVADTRQ LLWPIKRGQH LAQAKVWTIN
APEPMTTPTV RFYVK
//
