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CAZyme Information: MGYG000001461_01270

You are here: Home > Sequence: MGYG000001461_01270

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Bacteroides neonati
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides neonati
CAZyme ID MGYG000001461_01270
CAZy Family GT51
CAZyme Description Penicillin-binding protein 1A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
803 91086.79 8.1748
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001461 5024706 Isolate not provided not provided
Gene Location Start: 738935;  End: 741346  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001461_01270.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT51 94 280 1.5e-59 0.9887005649717514

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0744 MrcB 2.32e-155 64 757 33 613
Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
TIGR02074 PBP_1a_fam 6.92e-152 105 743 1 531
penicillin-binding protein, 1A family. Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of bifunctional transglycosylase/transpeptidase penicillin-binding proteins (PBP). In the Proteobacteria, this family includes PBP 1A but not the paralogous PBP 1B (TIGR02071). This family also includes related proteins, often designated PBP 1A, from other bacterial lineages. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
COG5009 MrcA 2.33e-139 67 744 28 722
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
PRK11636 mrcA 4.21e-80 89 741 49 785
penicillin-binding protein 1a; Provisional
TIGR02071 PBP_1b 4.27e-76 104 709 145 656
penicillin-binding protein 1B. Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of a particular bifunctional transglycosylase/transpeptidase in E. coli and other Proteobacteria, designated penicillin-binding protein 1B. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ADV43676.1 0.0 1 790 13 799
AVM56567.1 0.0 15 789 3 774
QIK54746.1 0.0 1 799 1 793
QIK60166.1 0.0 1 799 1 793
ADQ79385.1 0.0 35 766 42 775

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3UDF_A 1.39e-65 89 742 22 717
ChainA, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDF_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDI_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDI_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDX_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDX_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE0_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE0_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE1_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE1_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii]
4OON_A 7.57e-63 76 746 9 728
Crystalstructure of PBP1a in complex with compound 17 ((4Z,8S,11E,14S)-5-(2-amino-1,3-thiazol-4-yl)-14-(5,6-dihydroxy-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-8-formyl-2-methyl-6-oxo-3,10-dioxa-4,7,11-triazatetradeca-4,11-diene-2,12,14-tricarboxylic acid) [Pseudomonas aeruginosa PAO1]
5U2G_A 4.69e-58 71 637 5 569
2.6Angstrom Resolution Crystal Structure of Penicillin-Binding Protein 1A from Haemophilus influenzae [Haemophilus influenzae Rd KW20],5U2G_B 2.6 Angstrom Resolution Crystal Structure of Penicillin-Binding Protein 1A from Haemophilus influenzae [Haemophilus influenzae Rd KW20]
5FGZ_A 9.51e-42 118 712 168 670
E.coli PBP1b in complex with FPI-1465 [Escherichia coli K-12],5HL9_A E. coli PBP1b in complex with acyl-ampicillin and moenomycin [Escherichia coli K-12],5HLA_A E. coli PBP1b in complex with acyl-cephalexin and moenomycin [Escherichia coli K-12],5HLB_A E. coli PBP1b in complex with acyl-aztreonam and moenomycin [Escherichia coli K-12],5HLD_A E. coli PBP1b in complex with acyl-CENTA and moenomycin [Escherichia coli K-12],6YN0_A Structure of E. coli PBP1b with a FtsN peptide activating transglycosylase activity [Escherichia coli K-12],7LQ6_A Chain A, Penicillin-binding protein 1B [Escherichia coli K-12]
3VMA_A 1.09e-41 118 712 189 691
CrystalStructure of the Full-Length Transglycosylase PBP1b from Escherichia coli [Escherichia coli K-12]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O87626 6.74e-76 60 747 22 711
Penicillin-binding protein 1A OS=Neisseria flavescens OX=484 GN=mrcA PE=3 SV=1
P0A0Z5 2.33e-74 60 764 22 727
Penicillin-binding protein 1A OS=Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 / Z2491) OX=122587 GN=mrcA PE=3 SV=1
Q5FAC7 2.33e-74 60 764 22 727
Penicillin-binding protein 1A OS=Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090) OX=242231 GN=mrcA PE=3 SV=3
O05131 2.33e-74 60 764 22 727
Penicillin-binding protein 1A OS=Neisseria gonorrhoeae OX=485 GN=mrcA PE=1 SV=3
P0A0Z6 2.33e-74 60 764 22 727
Penicillin-binding protein 1A OS=Neisseria meningitidis serogroup B (strain MC58) OX=122586 GN=mrcA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.999908 0.000101 0.000001 0.000000 0.000000 0.000002

TMHMM  Annotations      download full data without filtering help

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