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CAZyme Information: MGYG000002873_00335

You are here: Home > Sequence: MGYG000002873_00335

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 CAG-495 sp900538765
Lineage Bacteria; Proteobacteria; Alphaproteobacteria; RF32; CAG-239; CAG-495; CAG-495 sp900538765
CAZyme ID MGYG000002873_00335
CAZy Family GT51
CAZyme Description Penicillin-binding protein 1C
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
758 MGYG000002873_3|CGC1 84092.62 8.654
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002873 1867269 MAG United States North America
Gene Location Start: 11455;  End: 13731  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002873_00335.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT51 44 195 3e-44 0.8587570621468926

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
TIGR02073 PBP_1c 0.0 17 755 1 727
penicillin-binding protein 1C. This subfamily of the penicillin binding proteins includes the member from E. coli designated penicillin-binding protein 1C. Members have both transglycosylase and transpeptidase domains and are involved in forming cross-links in the late stages of peptidoglycan biosynthesis. All members of this subfamily are presumed to have the same basic function. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
COG4953 PbpC 0.0 13 756 23 733
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis].
PRK11240 PRK11240 2.30e-111 48 750 61 767
penicillin-binding protein 1C; Provisional
TIGR02074 PBP_1a_fam 3.17e-97 48 544 1 521
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]
COG0744 MrcB 7.83e-97 3 576 27 619
Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AQQ01575.1 1.11e-220 1 757 17 786
ATC86697.1 3.47e-218 6 757 22 792
ABA87803.1 4.13e-216 13 757 20 775
ASQ45895.1 2.39e-215 15 755 26 767
BBO75930.1 2.64e-213 13 757 20 775

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5FGZ_A 5.79e-39 37 567 144 706
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 6.47e-39 37 567 165 727
CrystalStructure of the Full-Length Transglycosylase PBP1b from Escherichia coli [Escherichia coli K-12]
3FWL_A 8.07e-37 43 567 154 710
CrystalStructure of the Full-Length Transglycosylase PBP1b from Escherichia coli [Escherichia coli]
3UDF_A 1.21e-31 47 527 37 689
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]
3ZG8_B 6.41e-22 131 535 2 441
CrystalStructure of Penicillin Binding Protein 4 from Listeria monocytogenes in the Ampicillin bound form [Listeria monocytogenes],3ZG9_B Crystal Structure of Penicillin-Binding Protein 4 from Listeria monocytogenes in the Cefuroxime bound form [Listeria monocytogenes],3ZGA_B Crystal Structure of Penicillin-Binding Protein 4 from Listeria monocytogenes in the Carbenicillin bound form [Listeria monocytogenes]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P76577 2.44e-93 45 750 60 765
Penicillin-binding protein 1C OS=Escherichia coli (strain K12) OX=83333 GN=pbpC PE=1 SV=1
P38050 8.52e-43 52 542 70 586
Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
Q9KUC0 6.16e-41 49 532 180 696
Penicillin-binding protein 1B OS=Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) OX=243277 GN=mrcB PE=3 SV=1
P70997 2.81e-39 19 597 38 650
Penicillin-binding protein 2D OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpG PE=2 SV=3
A7FY32 1.94e-38 8 625 33 720
Penicillin-binding protein 1A OS=Clostridium botulinum (strain ATCC 19397 / Type A) OX=441770 GN=pbpA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.205133 0.789784 0.004024 0.000354 0.000301 0.000377

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002873_00335.