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3.A.5.1.1
General secretory pathway (Sec-SRP) complex.  A biphasic pulling force may act on TMSs during translocon-mediated membrane integration (Ismail et al. 2012).  Intermediate structures for the insertion of integral membrane proteins have been visualized (Bischoff et al. 2014).  Insertion of the Type II single span (N-terminus, in, C-terminus, out) protein, RodZ, requires only SecYEG, SecA and the pmf, but not SecB, SecDF, YidC or FtsY (Rawat et al. 2015).  The combined effects of ribosome and peptide binding to SecYEG may allow for co-translational membrane insertion of successive transmembrane segments (Ge et al. 2014). SecA penetrates deeply into the SecYEG channel during insertion, contacting transmembrane helices and periplasmic loops (Banerjee et al. 2017). A partially inserted nascent chain unzips the Sec translocon's lateral gate (Kater et al. 2019). Cardiolipin (CL) is required in vivo for the stability of the bacterial translocon (SecYEG) as well as its efficient function in co-translational insertion into and translocation across the inner membrane of E. coli (Ryabichko et al. 2020). PpiD (623 aas and 1 N-terminal TMS), a peptidyl-prolyl cis-trans isomerase D, and YfgM (206 aas and 1 N-terminal TMS) facilitate the transport of toxins into the E. coli cell in a SecY-dependent process (Jones et al. 2021). Synchronized real-time measurement of Sec-mediated protein translocation has been described (Gupta et al. 2021). An extracellular cutinase from Amycolatopsis mediterranei (AmCut) is able to degrade the plastics, polycaprolactone and polybutylene succinate (Tan et al. 2022). It is secreted from E. coli using the Sec system for export across the inner membrane, and possibly, a non-classical secretion pathway for export across the outer membrane (Tan et al. 2022).

Accession Number:P10121
Protein Name:Cell division protein FtsY aka B3464
Length:497
Molecular Weight:54513.00
Species:Escherichia coli [83333]
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Peripheral membrane protein2
Substrate protein polypeptide chain

Cross database links:

DIP: DIP-9709N
RefSeq: AP_004328.1    NP_417921.1   
Entrez Gene ID: 947978   
Pfam: PF00448    PF02881   
BioCyc: EcoCyc:EG10346-MONOMER    ECOL168927:B3464-MONOMER   
KEGG: ecj:JW3429    eco:b3464   

Gene Ontology

GO:0005886 C:plasma membrane
GO:0030529 C:ribonucleoprotein complex
GO:0005525 F:GTP binding
GO:0017111 F:nucleoside-triphosphatase activity
GO:0005515 F:protein binding
GO:0003723 F:RNA binding
GO:0007049 P:cell cycle
GO:0051301 P:cell division
GO:0006614 P:SRP-dependent cotranslational protein targe...

References (8)

[1] “A new cell division operon in Escherichia coli.”  Gill D.R.et.al.   3025556
[2] “Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes.”  Sofia H.J.et.al.   8041620
[3] “The complete genome sequence of Escherichia coli K-12.”  Blattner F.R.et.al.   9278503
[4] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.”  Hayashi K.et.al.   16738553
[5] “The identification of the Escherichia coli ftsY gene product: an unusual protein.”  Gill D.R.et.al.   2161989
[6] “An alternative protein targeting pathway in Escherichia coli: studies on the role of FtsY.”  Luirink J.et.al.   8194520
[7] “Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor.”  Buskiewicz I.et.al.   15148364
[8] “Crystal structure of the NG domain from the signal-recognition particle receptor FtsY.”  Montoya G.et.al.   9002525
Structure:
1FTS   2QY9   2XXA   2YHS   3ZN8   4C7O   5GAD   5NCO   5NIY   6CQP   [...more]

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MAKEKKRGFF SWLGFGQKEQ TPEKETEVQN EQPVVEEIVQ AQEPVKASEQ AVEEQPQAHT 
61:	EAEAETFAAD VVEVTEQVAE SEKAQPEAEV VAQPEPVVEE TPEPVAIERE ELPLPEDVNA 
121:	EAVSPEEWQA EAETVEIVEA AEEEAAKEEI TDEELETALA AEAAEEAVMV VPPAEEEQPV 
181:	EEIAQEQEKP TKEGFFARLK RSLLKTKENL GSGFISLFRG KKIDDDLFEE LEEQLLIADV 
241:	GVETTRKIIT NLTEGASRKQ LRDAEALYGL LKEEMGEILA KVDEPLNVEG KAPFVILMVG 
301:	VNGVGKTTTI GKLARQFEQQ GKSVMLAAGD TFRAAAVEQL QVWGQRNNIP VIAQHTGADS 
361:	ASVIFDAIQA AKARNIDVLI ADTAGRLQNK SHLMEELKKI VRVMKKLDVE APHEVMLTID 
421:	ASTGQNAVSQ AKLFHEAVGL TGITLTKLDG TAKGGVIFSV ADQFGIPIRY IGVGERIEDL 
481:	RPFKADDFIE ALFARED