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CAZyme Information: MGYG000003825_01299

You are here: Home > Sequence: MGYG000003825_01299

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 UBA1777 sp900549645
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; UBA1777; UBA1777 sp900549645
CAZyme ID MGYG000003825_01299
CAZy Family GT51
CAZyme Description Penicillin-binding protein 4
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
752 82802.92 4.1393
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003825 2022533 MAG United States North America
Gene Location Start: 14056;  End: 16314  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003825_01299.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT51 106 277 3.5e-66 0.96045197740113

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
TIGR02074 PBP_1a_fam 0.0 112 662 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]
COG0744 MrcB 3.59e-169 87 671 52 608
Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009 MrcA 1.83e-118 64 671 25 730
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
TIGR02071 PBP_1b 1.13e-91 111 660 145 683
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]
pfam00912 Transgly 5.95e-74 110 277 10 177
Transglycosylase. The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively. The transglycosylase domain catalyzes the polymerization of murein glycan chains.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ALP94484.1 1.40e-185 1 671 1 678
QBB65500.1 4.29e-185 45 671 3 646
QNL43378.1 2.72e-175 45 671 28 660
BAK99350.1 9.49e-172 42 671 29 684
BCK85139.1 3.25e-163 47 671 27 692

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3ZG8_B 1.97e-70 196 666 2 464
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]
3ZG7_B 1.80e-64 196 639 2 436
CrystalStructure of Penicillin-Binding Protein 4 from Listeria monocytogenes in the apo form [Listeria monocytogenes]
7U4H_A 8.75e-64 75 687 6 794
ChainA, Penicillin-binding protein 1A (Pbp1a) [Chlamydia trachomatis D/UW-3/CX],7U4H_B Chain B, Penicillin-binding protein 1A (Pbp1a) [Chlamydia trachomatis D/UW-3/CX]
4OON_A 1.86e-60 103 660 29 729
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]
3UDF_A 6.63e-54 116 638 42 691
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q0SRL7 1.14e-105 55 671 36 677
Penicillin-binding protein 1A OS=Clostridium perfringens (strain SM101 / Type A) OX=289380 GN=pbpA PE=3 SV=1
Q8XJ01 3.34e-103 54 667 35 673
Penicillin-binding protein 1A OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=pbpA PE=3 SV=1
A7FY32 1.14e-102 41 671 10 655
Penicillin-binding protein 1A OS=Clostridium botulinum (strain ATCC 19397 / Type A) OX=441770 GN=pbpA PE=3 SV=1
A5I6G4 1.14e-102 41 671 10 655
Penicillin-binding protein 1A OS=Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) OX=441771 GN=pbpA PE=3 SV=1
A7GHV1 7.90e-102 41 671 10 655
Penicillin-binding protein 1A OS=Clostridium botulinum (strain Langeland / NCTC 10281 / Type F) OX=441772 GN=pbpA 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
0.999950 0.000066 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

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