Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein translocase subunit SecDF

Gene

secDF

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Required for efficient translocation of secretory pre-proteins under conditions of hypersecretion but is not required for the release of mature proteins from the membrane.1 Publication
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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciBSUB:BSU27650-MONOMER.

Protein family/group databases

TCDBi2.A.6.4.2. the resistance-nodulation-cell division (rnd) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein translocase subunit SecDF
Gene namesi
Name:secDF
Ordered Locus Names:BSU27650
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

  • Note: Found uniformly distributed in both the mother cell and forespore following sporulation.

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 5Cytoplasmic1 Publication5
Transmembranei6 – 26HelicalSequence analysisAdd BLAST21
Topological domaini27 – 254Extracellular1 PublicationAdd BLAST228
Transmembranei255 – 275HelicalSequence analysisAdd BLAST21
Topological domaini276 – 278Cytoplasmic1 Publication3
Transmembranei279 – 299HelicalSequence analysisAdd BLAST21
Topological domaini300 – 301Extracellular1 Publication2
Transmembranei302 – 322HelicalSequence analysisAdd BLAST21
Topological domaini323 – 353Cytoplasmic1 PublicationAdd BLAST31
Transmembranei354 – 374HelicalSequence analysisAdd BLAST21
Topological domaini375 – 380Extracellular1 Publication6
Transmembranei381 – 401HelicalSequence analysisAdd BLAST21
Topological domaini402 – 453Cytoplasmic1 PublicationAdd BLAST52
Transmembranei454 – 474HelicalSequence analysisAdd BLAST21
Topological domaini475 – 569Extracellular1 PublicationAdd BLAST95
Transmembranei570 – 590HelicalSequence analysisAdd BLAST21
Topological domaini591 – 593Cytoplasmic1 Publication3
Transmembranei594 – 614HelicalSequence analysisAdd BLAST21
Topological domaini615 – 621Extracellular1 Publication7
Transmembranei622 – 642HelicalSequence analysisAdd BLAST21
Topological domaini643 – 677Cytoplasmic1 PublicationAdd BLAST35
Transmembranei678 – 698HelicalSequence analysisAdd BLAST21
Topological domaini699Extracellular1 Publication1
Transmembranei700 – 720HelicalSequence analysisAdd BLAST21
Topological domaini721 – 737Cytoplasmic1 PublicationAdd BLAST17

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene show a cold-sensitive phenotype and a filamentous morphology.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003844021 – 737Protein translocase subunit SecDFAdd BLAST737

Proteomic databases

PaxDbiO32047.

Expressioni

Inductioni

Shows maximal expression at the beginning of post-exponential growth phase and increased expression by glucose in the post-exponential growth phase when cells are cultured on rich medium. Expressed constitutively during growth in minimal medium.1 Publication

Interactioni

Subunit structurei

Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary protein SecDF. Other proteins may also be involved (By similarity).By similarity

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100015111.

Structurei

3D structure databases

ProteinModelPortaliO32047.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 416SecDAdd BLAST416
Regioni446 – 737SecFAdd BLAST292

Sequence similaritiesi

In the N-terminal section; belongs to the SecD/SecF family. SecD subfamily.Curated
In the C-terminal section; belongs to the SecD/SecF family. SecF subfamily.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C3D. Bacteria.
COG0341. LUCA.
COG0342. LUCA.
HOGENOMiHOG000018636.
InParanoidiO32047.
KOiK12257.
OMAiLLLGNWW.
PhylomeDBiO32047.

Family and domain databases

HAMAPiMF_01463_B. SecD_B. 1 hit.
MF_01464_B. SecF_B. 1 hit.
InterProiIPR005791. SecD.
IPR022813. SecD/SecF_arch_bac.
IPR022645. SecD/SecF_bac.
IPR022646. SecD/SecF_CS.
IPR005665. SecF_bac.
[Graphical view]
PfamiPF07549. Sec_GG. 1 hit.
PF02355. SecD_SecF. 2 hits.
[Graphical view]
PRINTSiPR01755. SECFTRNLCASE.
TIGRFAMsiTIGR00916. 2A0604s01. 2 hits.
TIGR00966. 3a0501s07. 1 hit.
TIGR01129. secD. 1 hit.

Sequencei

Sequence statusi: Complete.

O32047-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKGRLIAFF LFVLLIGTGL GYFTKPAANN ITLGLDLQGG FEVLYDVQPV
60 70 80 90 100
KKGDKITKDV LVSTVEALNR RANVLGVSEP NIQIEGNNRI RVQLAGVTNQ
110 120 130 140 150
NRAREILATE AQLSFRDAND KELLNGADLV ENGAKQTYDS TTNEPIVTIK
160 170 180 190 200
LKDADKFGEV TKKVMKMAPN NQLVIWLDYD KGDSFKKEVQ KEHPKFVSAP
210 220 230 240 250
NVSQELNTTD VKIEGHFTAQ EAKDLASILN AGALPVKLTE KYSTSVGAQF
260 270 280 290 300
GQQALHDTVF AGIVGIAIIF LFMLFYYRLP GLIAVITLSV YIYITLQIFD
310 320 330 340 350
WMNAVLTLPG IAALILGVGM AVDANIITYE RIKEELKLGK SVRSAFRSGN
360 370 380 390 400
RRSFATIFDA NITTIIAAVV LFIFGTSSVK GFATMLILSI LTSFITAVFL
410 420 430 440 450
SRFLLALLVE SRWLDRKKGW FGVNKKHIMD IQDTDENTEP HTPFQKWDFT
460 470 480 490 500
SKRKYFFIFS SAVTVAGIII LLVFRLNLGI DFASGARIEV QSDHKLTTEQ
510 520 530 540 550
VEKDFESLGM DPDTVVLSGE KSNIGVARFV GVPDKETIAK VKTYFKDKYG
560 570 580 590 600
SDPNVSTVSP TVGKELARNA LYAVAIASIG IIIYVSIRFE YKMAIAAIAS
610 620 630 640 650
LLYDAFFIVT FFSITRLEVD VTFIAAILTI IGYSINDTIV TFDRVREHMK
660 670 680 690 700
KRKPKTFADL NHIVNLSLQQ TFTRSINTVL TVVIVVVTLL IFGASSITNF
710 720 730
SIALLVGLLT GVYSSLYIAA QIWLAWKGRE LKKDSAQ
Length:737
Mass (Da):81,654
Last modified:August 1, 1999 - v2
Checksum:i54C397E939779177
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF024506 Genomic DNA. Translation: AAC31122.1.
AL009126 Genomic DNA. Translation: CAB14724.2.
PIRiH69704.
RefSeqiNP_390643.1. NC_000964.3.
WP_003245970.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14724; CAB14724; BSU27650.
GeneIDi937938.
KEGGibsu:BSU27650.
PATRICi18977394. VBIBacSub10457_2886.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF024506 Genomic DNA. Translation: AAC31122.1.
AL009126 Genomic DNA. Translation: CAB14724.2.
PIRiH69704.
RefSeqiNP_390643.1. NC_000964.3.
WP_003245970.1. NZ_JNCM01000036.1.

3D structure databases

ProteinModelPortaliO32047.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100015111.

Protein family/group databases

TCDBi2.A.6.4.2. the resistance-nodulation-cell division (rnd) superfamily.

Proteomic databases

PaxDbiO32047.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14724; CAB14724; BSU27650.
GeneIDi937938.
KEGGibsu:BSU27650.
PATRICi18977394. VBIBacSub10457_2886.

Phylogenomic databases

eggNOGiENOG4105C3D. Bacteria.
COG0341. LUCA.
COG0342. LUCA.
HOGENOMiHOG000018636.
InParanoidiO32047.
KOiK12257.
OMAiLLLGNWW.
PhylomeDBiO32047.

Enzyme and pathway databases

BioCyciBSUB:BSU27650-MONOMER.

Family and domain databases

HAMAPiMF_01463_B. SecD_B. 1 hit.
MF_01464_B. SecF_B. 1 hit.
InterProiIPR005791. SecD.
IPR022813. SecD/SecF_arch_bac.
IPR022645. SecD/SecF_bac.
IPR022646. SecD/SecF_CS.
IPR005665. SecF_bac.
[Graphical view]
PfamiPF07549. Sec_GG. 1 hit.
PF02355. SecD_SecF. 2 hits.
[Graphical view]
PRINTSiPR01755. SECFTRNLCASE.
TIGRFAMsiTIGR00916. 2A0604s01. 2 hits.
TIGR00966. 3a0501s07. 1 hit.
TIGR01129. secD. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSECDF_BACSU
AccessioniPrimary (citable) accession number: O32047
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: August 1, 1999
Last modified: September 7, 2016
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.