CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003596
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein translocase subunit SecD 
Protein Synonyms/Alias
  
Gene Name
 secD 
Gene Synonyms/Alias
 b0408; JW0398 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
608VNLLYGGKRVKKLSIacetylation[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
 Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. The large periplasmic domain is thought to have a base and head domain joined by a hinge; movement of the hinge may be coupled to both proton transport and protein export, with the head domain capturing substrate, and a conformational change preventing backward movement and driving forward movement. Expression of V.alginolyticus SecD and SecF in E.coli confers Na(+)-dependent protein export, strongly suggesting SecDF functions via cation-coupled protein translocation. 
Sequence Annotation
 REGION 279 426 Required for protein export.  
Keyword
 Cell inner membrane; Cell membrane; Complete proteome; Membrane; Protein transport; Reference proteome; Translocation; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 615 AA 
Protein Sequence
MLNRYPLWKY VMLIVVIVIG LLYALPNLFG EDPAVQITGA RGVAASEQTL IQVQKTLQEE 60
KITAKSVALE EGAILARFDS TDTQLRAREA LMGVMGDKYV VALNLAPATP RWLAAIHAEP 120
MKLGLDLRGG VHFLMEVDMD TALGKLQEQN IDSLRSDLRE KGIPYTTVRK ENNYGLSITF 180
RDAKARDEAI AYLSKRHPDL VISSQGSNQL RAVMSDARLS EAREYAVQQN INILRNRVNQ 240
LGVAEPVVQR QGADRIVVEL PGIQDTARAK EILGATATLE FRLVNTNVDQ AAAASGRVPG 300
DSEVKQTREG QPVVLYKRVI LTGDHITDST SSQDEYNQPQ VNISLDSAGG NIMSNFTKDN 360
IGKPMATLFV EYKDSGKKDA NGRAVLVKQE EVINIANIQS RLGNSFRITG INNPNEARQL 420
SLLLRAGALI APIQIVEERT IGPTLGMQNI EQGLEACLAG LLVSILFMII FYKKFGLIAT 480
SALIANLILI VGIMSLLPGA TLSMPGIAGI VLTLAVAVDA NVLINERIKE ELSNGRTVQQ 540
AIDEGYRGAF SSIFDANITT LIKVIILYAV GTGAIKGFAI TTGIGVATSM FTAIVGTRAI 600
VNLLYGGKRV KKLSI 615 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro.
 GO:0065002; P:intracellular protein transmembrane transport; IEA:HAMAP.
 GO:0006605; P:protein targeting; IEA:HAMAP.
 GO:0015031; P:protein transport; IMP:EcoliWiki.
 GO:0043952; P:protein transport by the Sec complex; IEA:HAMAP. 
Interpro
 IPR005791; SecD.
 IPR027398; SecD-TM.
 IPR022813; SecD/SecF_arch_bac.
 IPR022645; SecD/SecF_bac.
 IPR022646; SecD/SecF_CS. 
Pfam
 PF07549; Sec_GG
 PF13721; SecD-TM1
 PF02355; SecD_SecF 
SMART
  
PROSITE
  
PRINTS