| Tag | Content |
|---|
| CPLM ID | CPLM-002024 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Penicillin-binding protein 1B |
Protein Synonyms/Alias | PBP-1b; PBP1b; Murein polymerase; Penicillin-insensitive transglycosylase; Peptidoglycan TGase; Peptidoglycan glycosyltransferase; Penicillin-sensitive transpeptidase; DD-transpeptidase |
Gene Name | mrcB |
Gene Synonyms/Alias | pbpF; ponB; b0149; JW0145 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 689 | TGRQLGAKYPNLHLA | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). |
Sequence Annotation | REGION 88 250 Membrane association.
REGION 109 200 UvrB domain 2 homolog.
REGION 195 367 Transglycosylase.
REGION 444 736 Transpeptidase.
ACT_SITE 233 233 Proton donor; for transglycosylase
ACT_SITE 510 510 Acyl-ester intermediate; for |
Keyword | 3D-structure; Alternative initiation; Antibiotic resistance; Cell inner membrane; Cell membrane; Cell shape; Cell wall biogenesis/degradation; Complete proteome; Direct protein sequencing; Glycosyltransferase; Hydrolase; Membrane; Multifunctional enzyme; Peptidoglycan synthesis; Reference proteome; Signal-anchor; Transferase; Transmembrane; Transmembrane helix. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 844 AA |
Protein Sequence | MAGNDREPIG RKGKPTRPVK QKVSRRRYED DDDYDDYDDY EDEEPMPRKG KGKGKGRKPR 60
GKRGWLWLLL KLAIVFAVLI AIYGVYLDQK IRSRIDGKVW QLPAAVYGRM VNLEPDMTIS 120
KNEMVKLLEA TQYRQVSKMT RPGEFTVQAN SIEMIRRPFD FPDSKEGQVR ARLTFDGDHL 180
ATIVNMENNR QFGFFRLDPR LITMISSPNG EQRLFVPRSG FPDLLVDTLL ATEDRHFYEH 240
DGISLYSIGR AVLANLTAGR TVQGASTLTQ QLVKNLFLSS ERSYWRKANE AYMALIMDAR 300
YSKDRILELY MNEVYLGQSG DNEIRGFPLA SLYYFGRPVE ELSLDQQALL VGMVKGASIY 360
NPWRNPKLAL ERRNLVLRLL QQQQIIDQEL YDMLSARPLG VQPRGGVISP QPAFMQLVRQ 420
ELQAKLGDKV KDLSGVKIFT TFDSVAQDAA EKAAVEGIPA LKKQRKLSDL ETAIVVVDRF 480
SGEVRAMVGG SEPQFAGYNR AMQARRSIGS LAKPATYLTA LSQPKIYRLN TWIADAPIAL 540
RQPNGQVWSP QNDDRRYSES GRVMLVDALT RSMNVPTVNL GMALGLPAVT ETWIKLGVPK 600
DQLHPVPAML LGALNLTPIE VAQAFQTIAS GGNRAPLSAL RSVIAEDGKV LYQSFPQAER 660
AVPAQAAYLT LWTMQQVVQR GTGRQLGAKY PNLHLAGKTG TTNNNVDTWF AGIDGSTVTI 720
TWVGRDNNQP TKLYGASGAM SIYQRYLANQ TPTPLNLVPP EDIADMGVDY DGNFVCSGGM 780
RILPVWTSDP QSLCQQSEMQ QQPSGNPFDQ SSQPQQQPQQ QPAQQEQKDS DGVAGWIKDM 840
FGSN 844 |
Gene Ontology | GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0016020; C:membrane; IDA:UniProtKB. GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro. GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. GO:0008658; F:penicillin binding; IDA:EcoCyc. GO:0008955; F:peptidoglycan glycosyltransferase activity; IDA:EcoCyc. GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IDA:EcoCyc. GO:0009252; P:peptidoglycan biosynthetic process; IGI:EcoCyc. GO:0008360; P:regulation of cell shape; IGI:EcoCyc. GO:0046677; P:response to antibiotic; IGI:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |