ID E3GBQ7_ENTLS Unreviewed; 850 AA.
AC E3GBQ7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Penicillin-binding protein 1A {ECO:0000256|ARBA:ARBA00018638};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN OrderedLocusNames=Entcl_0338 {ECO:0000313|EMBL:ADO46616.1};
OS Enterobacter lignolyticus (strain SCF1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Pluralibacter.
OX NCBI_TaxID=701347 {ECO:0000313|EMBL:ADO46616.1, ECO:0000313|Proteomes:UP000006872};
RN [1] {ECO:0000313|Proteomes:UP000006872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCF1 {ECO:0000313|Proteomes:UP000006872};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA Mikhailova N., DeAngelis K., Arkin A.P., Chivian D., Edwards B., Woo H.,
RA Hazen T.C., Woyke T.;
RT "Complete sequence of Enterobacter cloacae SCF1.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO46616.1, ECO:0000313|Proteomes:UP000006872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCF1 {ECO:0000313|EMBL:ADO46616.1,
RC ECO:0000313|Proteomes:UP000006872};
RX PubMed=22180812; DOI=10.4056/sigs.2104875;
RA Deangelis K.M., D'Haeseleer P., Chivian D., Fortney J.L., Khudyakov J.,
RA Simmons B., Woo H., Arkin A.P., Davenport K.W., Goodwin L., Chen A.,
RA Ivanova N., Kyrpides N.C., Mavromatis K., Woyke T., Hazen T.C.;
RT "Complete genome sequence of "Enterobacter lignolyticus" SCF1.";
RL Stand. Genomic Sci. 5:69-85(2011).
CC -!- FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan
CC from the lipid intermediates. The enzyme has a penicillin-insensitive
CC transglycosylase N-terminal domain (formation of linear glycan strands)
CC and a penicillin-sensitive transpeptidase C-terminal domain (cross-
CC linking of the peptide subunits). {ECO:0000256|ARBA:ARBA00002624}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004249}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004249}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
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; CP002272; ADO46616.1; -; Genomic_DNA.
DR RefSeq; WP_013364394.1; NC_014618.1.
DR AlphaFoldDB; E3GBQ7; -.
DR STRING; 701347.Entcl_0338; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; esc:Entcl_0338; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000006872; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase 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 GO; GO:0046677; P:response to antibiotic; 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; IPR031376; PCB_OB.
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:SF27; PENICILLIN-BINDING PROTEIN 1A; 1.
DR Pfam; PF17092; PCB_OB; 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 Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000313|EMBL:ADO46616.1};
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:UP000006872};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000313|EMBL:ADO46616.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 55..229
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 316..425
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 429..605
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 850 AA; 93377 MW; 55FCB6C31099B83A CRC64;
MKFVKYLFIL AVCCILLGAG SIYGLYKYIE PQLPDVATLR DVRLQIPMQV YSAEGELIAQ
YGEKRRIPVT LNQIPPTLVK AFIATEDSRF YEHHGVDPVG IFRAASVALF SGHASQGAST
ITQQLARNFF LSPEKTLMRK IKEAFLAIRI EQLLNKDEIL ELYLNKIYLG YRAYGVGAAA
QVYFGKTVDQ LTLNEMAVIA GLPKAPSTFN PLYSMDRATA RRNVVLSRML SEGYITQAQY
DETSREPIDA SYHAPEIAFS APYLTEMVRQ EMVNRYGDKA YEDGYRIYTT ITRKDQLAAQ
QAVRNNVMDY DMRHGYRGPA NVLWKVGETP WDSKKITDSL KSLPTYGPLE PAVVTATGPQ
EATVMMADGT SAALSMDGMR WARPYRSDTL QGATPRKVTD VVQTGQQIWI RQVNNSWWLA
QVPDVNSALV SVNPQNGAII ALVGGFDFNQ SKFNRATQAL RQVGSNIKPF LYTAAMDKGL
TLASVLNDVP ISRWDAGAGS DWRPKNSPPE YAGPIRLRQG LGQSKNVVMV RAMRAMGVDY
AAEYLQRFGF PADNIVHTES LALGSASFTP LQVARGYSVM ANGGFLIDPY FISKIENDQG
NVLFEAKPKI ACADCDIPVI YGDTPKSNVL ENKDVEDVAI SQEPQNANVP MPSLEQANQA
LVARSGGQEY APHVISTPLA FLIKSALNTN IFGEPGWQGT GWRAGRDLQR KDIGGKTGTT
NSSKDAWFSG YGPGVVTSVW IGFDDHRRDL GRTTASGAIK DQISGYEGGA KSAQPAWDAF
MKSVLQGVPE QPLTPPTGVV TVNIDRSTGQ LANGGNSREE YFIEGTQPTQ QAVHEVGTTL
IDNGETHELF
//
