CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004125
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Periplasmic trehalase 
Protein Synonyms/Alias
 Alpha,alpha-trehalase; Alpha,alpha-trehalose glucohydrolase; Tre37A 
Gene Name
 treA 
Gene Synonyms/Alias
 osmA; b1197; JW1186 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
135RSTENTEKWDSLLPLacetylation[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
 Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system. 
Sequence Annotation
 REGION 159 160 Substrate binding (Probable).
 REGION 205 207 Substrate binding (Probable).
 REGION 277 279 Substrate binding (Probable).
 ACT_SITE 312 312 Proton donor/acceptor (By similarity).
 ACT_SITE 496 496 Proton donor/acceptor (By similarity).
 BINDING 152 152 Substrate (Probable).
 BINDING 196 196 Substrate (Probable).
 BINDING 310 310 Substrate; via carbonyl oxygen
 BINDING 511 511 Substrate (Probable).  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; Glycosidase; Hydrolase; Periplasm; Reference proteome; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 565 AA 
Protein Sequence
MKSPAPSRPQ KMALIPACIF LCFAALSVQA EETPVTPQPP DILLGPLFND VQNAKLFPDQ 60
KTFADAVPNS DPLMILADYR MQQNQSGFDL RHFVNVNFTL PKEGEKYVPP EGQSLREHID 120
GLWPVLTRST ENTEKWDSLL PLPEPYVVPG GRFREVYYWD SYFTMLGLAE SGHWDKVADM 180
VANFAHEIDT YGHIPNGNRS YYLSRSQPPF FALMVELLAQ HEGDAALKQY LPQMQKEYAY 240
WMDGVENLQA GQQEKRVVKL QDGTLLNRYW DDRDTPRPES WVEDIATAKS NPNRPATEIY 300
RDLRSAAASG WDFSSRWMDN PQQLNTLRTT SIVPVDLNSL MFKMEKILAR ASKAAGDNAM 360
ANQYETLANA RQKGIEKYLW NDQQGWYADY DLKSHKVRNQ LTAAALFPLY VNAAAKDRAN 420
KMATATKTHL LQPGGLNTTS VKSGQQWDAP NGWAPLQWVA TEGLQNYGQK EVAMDISWHF 480
LTNVQHTYDR EKKLVEKYDV STTGTGGGGG EYPLQDGFGW TNGVTLKMLD LICPKEQPCD 540
NVPATRPTVK SATTQPSTKE AQPTP 565 
Gene Ontology
 GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
 GO:0004555; F:alpha,alpha-trehalase activity; IDA:UniProtKB.
 GO:0071474; P:cellular hyperosmotic response; IEP:EcoCyc.
 GO:0006974; P:response to DNA damage stimulus; IEP:EcoliWiki.
 GO:0005993; P:trehalose catabolic process; IDA:UniProtKB. 
Interpro
 IPR008928; 6-hairpin_glycosidase-like.
 IPR001661; Glyco_hydro_37.
 IPR018232; Glyco_hydro_37_CS.
 IPR023720; Trehalase_periplasmic. 
Pfam
 PF01204; Trehalase 
SMART
  
PROSITE
 PS00927; TREHALASE_1
 PS00928; TREHALASE_2 
PRINTS
 PR00744; GLHYDRLASE37.