ID M1LZA9_9PROT Unreviewed; 769 AA.
AC M1LZA9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Penicillin-binding protein 1A {ECO:0000313|EMBL:AGF49401.1};
DE EC=2.4.1.- {ECO:0000313|EMBL:AGF49401.1};
GN ORFNames=ST1E_0155 {ECO:0000313|EMBL:AGF49401.1};
OS Candidatus Kinetoplastibacterium galatii TCC219.
OC Bacteria; Pseudomonadota; Betaproteobacteria;
OC Candidatus Kinetoplastibacterium.
OX NCBI_TaxID=1208921 {ECO:0000313|EMBL:AGF49401.1, ECO:0000313|Proteomes:UP000011658};
RN [1] {ECO:0000313|EMBL:AGF49401.1, ECO:0000313|Proteomes:UP000011658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCC219 {ECO:0000313|EMBL:AGF49401.1,
RC ECO:0000313|Proteomes:UP000011658};
RX PubMed=23345457;
RA Alves J.M., Serrano M.G., Maia da Silva F., Voegtly L.J., Matveyev A.V.,
RA Teixeira M.M., Camargo E.P., Buck G.A.;
RT "Genome evolution and phylogenomic analysis of candidatus
RT kinetoplastibacterium, the betaproteobacterial endosymbionts of strigomonas
RT and angomonas.";
RL Genome Biol. Evol. 5:338-350(2013).
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 -!- 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; CP003806; AGF49401.1; -; Genomic_DNA.
DR RefSeq; WP_015389885.1; NC_020284.1.
DR AlphaFoldDB; M1LZA9; -.
DR STRING; 1208921.ST1E_0155; -.
DR KEGG; kga:ST1E_0155; -.
DR PATRIC; fig|1208921.3.peg.694; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_4; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000011658; Chromosome.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; 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 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; 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 Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosyltransferase {ECO:0000313|EMBL:AGF49401.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transferase {ECO:0000313|EMBL:AGF49401.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..236
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 429..693
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 769 AA; 87647 MW; 015B91665338AA48 CRC64;
MKQKYILPKF LINIITISLS ILAIIIFVIC ILISLTWRKL PDLSAMIDYK PRIPLRIYSS
DNILIGEFGE ERRSVLNFQD IPNIMKLSIL AAEDDRFYKH GGIDWIGIVR AGLINLKNMS
KTQGASTITM QLARNFYLSS EKTYSRKLYE LMLTLKIESE LTKNKILELY MNQIYLGNRA
YGFAAASLVY FNKPLSEINL AESAMLAGIP KAPSIFNPIS NFKRTKLRQN YVLKRMISLG
YITMNEYREA IDTDVKIYNA FKKQHVYEVH GEYVAELVRQ LLFKNFKSDL YSKGINVYTT
IRSKDQDSAY KAVRKVVIDY TKTKYLGPED QIEIPIELDI SSILSGNRIT EIFDKYNDSD
EISAALVISA NDEYITAIKK DKVIVKINKA NSNINNNELS KEIKRGSIIH LYKDKEELRI
INMPTLQAAF VSISPQDGRI LSLVGGFDFY RGNFNRVTQA WRQPGSSIKP FIYASAIEKG
ISPATRISDL PLIMTAEQTG SKAWNPKNYG HRYEKDMVSM RNGLYKSKNM VSIRILQNIG
PEYARNYLEK FGFDKSRQPA VISLALGTGL VTPLQLTSAF SIFANEGHLI PPYLIEKVTD
SYGRTIMQHN KIRPNKSNQA IDSRVAYIMN DILRGVVKHG TASKAKKALR RDDIAGKTGT
TNDSVDAWFS GYTKDIVATA WVGFDQPKSL GSNETGSNIA MPVWINYMKD VIRNYPEQEE
KKVPEGIIVY NNELYLKEFP PEIAISEIKP SEEFYDEELR NVIQNRFEN
//
