ID A0A097QZH8_HAFAL Unreviewed; 775 AA.
AC A0A097QZH8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=AT03_05375 {ECO:0000313|EMBL:AIU71873.1};
OS Hafnia alvei FB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Hafnia.
OX NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU71873.1, ECO:0000313|Proteomes:UP000029986};
RN [1] {ECO:0000313|EMBL:AIU71873.1, ECO:0000313|Proteomes:UP000029986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB1 {ECO:0000313|EMBL:AIU71873.1,
RC ECO:0000313|Proteomes:UP000029986};
RX PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA Tan J.Y., Yin W.F., Chan K.G.;
RT "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT pathogenesis: a draft genome perspective.";
RL Gut Pathog. 6:29-29(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; CP009706; AIU71873.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A097QZH8; -.
DR KEGG; hav:AT03_05375; -.
DR PATRIC; fig|1453496.5.peg.1068; -.
DR eggNOG; COG4953; Bacteria.
DR HOGENOM; CLU_006354_7_3_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000029986; 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; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 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:UP000029986}.
FT DOMAIN 61..227
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 332..522
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 694..770
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 775 AA; 86347 MW; AB3ADDD8DB99C5F5 CRC64;
MRMSLKRLRK WCVIIALLAL LICSGLWLAD KVWPLPLSDV QVARVVVAED GSPLWRFADG
QGVWRYPITI KQVSPYYLQA LLTYEDRWFY KHPGINPFAI ARAAWQDLSH GEIISGGSTL
SMQVARLLDP HPRTFGGKVR QIWRTAQLEW YLSKTQILEL YLNRAPFGGT LQGIGAASWA
YLGKPPDELT RGEAALLAVL PQAPSRLRPD RYPERAQAAR NKVLDRLVQY QVWTKQQADD
VKQEPVWLAS RQMPQTAPLL ARRMVQTYPH QDVIETTIDA ALQRQLETLA QGWLSRLPAK
TSVGVLIVDH TDMQVKAYLG SLNFADRSRF GYVDMVSAWR SPGSTLKPFL YGLALDDGII
HNESLLQDVP RRFGDYRPGN FDTGFHGAVA ASEALTRSLN LPAVQLMEAY GPKRFTAELR
NAGLTLRFPA YAEPNLSLIL GGAGIRLDQL VSAYSALARH GQSADLRFVP TKKIHNRPLM
SPGAAWIIRR TLAGQARPEP DDSLSAVVPL AWKTGTSFGY RDAWAVGLNA RYTIGVWVGR
PDGTPVAGQF GYATAIPLLF QLNNLLLNNP RLRGNGWPTD PRPRSVSSAV ICWPGGQPLN
AQDTNCRQRR SAWILDGTIP PTLVAPGQES SQGIWRRQWL NDKGERVAPE CVGAVEKKLA
LWPLPLEPWL PEAEKRSHRL PMASQTCPPP IETASAPLIL IGLNNGSILR RPPGKTRIDL
RLTTQGGIGE RWWFLNGELV SQEPQFTYSF TRAGRYQLTV MDDGGQLTSA DFQVE
//
