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Protein

Protein translocase subunit SecA

Gene

secA

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

Functioni

Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: May bind 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi825 – 8251ZincUniRule annotation
Metal bindingi827 – 8271ZincUniRule annotation
Metal bindingi836 – 8361ZincUniRule annotation
Metal bindingi837 – 8371ZincUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi100 – 1078ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU35300-MONOMER.
BRENDAi3.6.3.B1. 658.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein translocase subunit SecAUniRule annotation
Gene namesi
Name:secAUniRule annotation
Synonyms:div+
Ordered Locus Names:BSU35300
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cell membrane UniRule annotation; Peripheral membrane protein UniRule annotation; Cytoplasmic side UniRule annotation
  • Cytoplasm

  • Note: Distribution is 50-50.UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi587 – 5871G → C: Forms position 587-750 dimers upon oxidation in vitro; when associated with C-750. Does not form position 587-587 dimers (homodimers). 1 Publication
Mutagenesisi588 – 5881N → C: Forms position 588-588 dimers upon oxidation in vitro (homodimers). 1 Publication
Mutagenesisi750 – 7501R → C: Forms position 587-750 dimers upon oxidation in vitro; when associated with C-587. Also forms position 750-750 dimers (homodimers). 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 841841Protein translocase subunit SecAPRO_0000109576Add
BLAST

Proteomic databases

PaxDbiP28366.

Interactioni

Subunit structurei

Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may be involved. Monomer and many different homodimers can be isolated (PubMed:16989859), some of which are not formed in the presence of a synthetic signal peptide. A single SecA monomer interacts with SecY in the channel.2 Publications

Protein-protein interaction databases

DIPiDIP-59805N.
IntActiP28366. 2 interactions.
MINTiMINT-8365061.
STRINGi224308.Bsubs1_010100019096.

Structurei

Secondary structure

841
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 66Combined sources
Beta strandi12 – 143Combined sources
Helixi18 – 2811Combined sources
Helixi31 – 344Combined sources
Helixi38 – 5316Combined sources
Helixi58 – 7720Combined sources
Helixi83 – 9311Combined sources
Beta strandi96 – 994Combined sources
Helixi106 – 11813Combined sources
Turni119 – 1224Combined sources
Beta strandi124 – 1307Combined sources
Helixi131 – 14717Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi157 – 1593Combined sources
Helixi161 – 1699Combined sources
Beta strandi170 – 1767Combined sources
Helixi177 – 18711Combined sources
Helixi193 – 1953Combined sources
Beta strandi203 – 2075Combined sources
Helixi209 – 2135Combined sources
Turni214 – 2185Combined sources
Beta strandi220 – 2289Combined sources
Helixi232 – 24110Combined sources
Turni242 – 2443Combined sources
Beta strandi246 – 2505Combined sources
Beta strandi254 – 2563Combined sources
Beta strandi258 – 2614Combined sources
Helixi263 – 27210Combined sources
Turni275 – 2773Combined sources
Beta strandi278 – 2803Combined sources
Helixi281 – 2833Combined sources
Helixi284 – 29815Combined sources
Turni302 – 3043Combined sources
Beta strandi305 – 3095Combined sources
Beta strandi312 – 3165Combined sources
Turni318 – 3203Combined sources
Helixi330 – 3323Combined sources
Helixi333 – 3408Combined sources
Beta strandi349 – 3568Combined sources
Helixi357 – 3615Combined sources
Beta strandi364 – 3729Combined sources
Helixi375 – 3773Combined sources
Helixi378 – 3858Combined sources
Beta strandi389 – 3913Combined sources
Beta strandi399 – 4024Combined sources
Beta strandi406 – 4105Combined sources
Helixi411 – 42717Combined sources
Beta strandi432 – 4376Combined sources
Helixi439 – 45012Combined sources
Turni451 – 4533Combined sources
Beta strandi457 – 4593Combined sources
Beta strandi461 – 4633Combined sources
Helixi464 – 4718Combined sources
Turni472 – 4754Combined sources
Beta strandi480 – 4845Combined sources
Turni485 – 4906Combined sources
Turni497 – 4993Combined sources
Helixi500 – 5023Combined sources
Beta strandi504 – 5118Combined sources
Helixi516 – 5238Combined sources
Helixi528 – 5303Combined sources
Beta strandi533 – 5408Combined sources
Helixi545 – 5473Combined sources
Helixi550 – 56112Combined sources
Beta strandi565 – 5673Combined sources
Helixi572 – 61847Combined sources
Beta strandi621 – 6233Combined sources
Helixi624 – 64118Combined sources
Beta strandi645 – 6484Combined sources
Helixi649 – 6513Combined sources
Helixi657 – 6626Combined sources
Turni663 – 6653Combined sources
Beta strandi668 – 6714Combined sources
Beta strandi672 – 6754Combined sources
Helixi681 – 70222Combined sources
Turni704 – 7063Combined sources
Helixi707 – 73630Combined sources
Helixi738 – 7403Combined sources
Beta strandi744 – 7463Combined sources
Helixi748 – 77629Combined sources
Beta strandi794 – 7974Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M6NX-ray2.70A1-802[»]
1M74X-ray3.00A1-802[»]
1TF2X-ray2.90A1-841[»]
1TF5X-ray2.18A1-841[»]
2IBMX-ray3.20A/B1-780[»]
3DL8X-ray7.50A/B1-779[»]
3IQMX-ray3.40A1-802[»]
3IQYX-ray3.30A1-841[»]
3JV2X-ray2.50A/B1-780[»]
5EULX-ray3.70A1-741[»]
A744-780[»]
ProteinModelPortaliP28366.
SMRiP28366. Positions 1-802.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28366.

Family & Domainsi

Sequence similaritiesi

Belongs to the SecA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0653. LUCA.
HOGENOMiHOG000218169.
InParanoidiP28366.
KOiK03070.
OMAiIATERHE.
OrthoDBiEOG654P48.
PhylomeDBiP28366.

Family and domain databases

Gene3Di1.10.3060.10. 1 hit.
3.40.50.300. 3 hits.
3.90.1440.10. 1 hit.
HAMAPiMF_01382. SecA.
InterProiIPR027417. P-loop_NTPase.
IPR004027. SEC_C_motif.
IPR000185. SecA.
IPR020937. SecA_CS.
IPR011115. SecA_DEAD.
IPR014018. SecA_motor_DEAD.
IPR011130. SecA_preprotein_X-link_dom.
IPR011116. SecA_Wing/Scaffold.
[Graphical view]
PfamiPF02810. SEC-C. 1 hit.
PF07517. SecA_DEAD. 1 hit.
PF01043. SecA_PP_bind. 1 hit.
PF07516. SecA_SW. 1 hit.
[Graphical view]
PRINTSiPR00906. SECA.
SMARTiSM00957. SecA_DEAD. 1 hit.
SM00958. SecA_PP_bind. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
SSF81767. SSF81767. 1 hit.
SSF81886. SSF81886. 2 hits.
TIGRFAMsiTIGR00963. secA. 1 hit.
PROSITEiPS01312. SECA. 1 hit.
PS51196. SECA_MOTOR_DEAD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P28366-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGILNKMFD PTKRTLNRYE KIANDIDAIR GDYENLSDDA LKHKTIEFKE
60 70 80 90 100
RLEKGATTDD LLVEAFAVVR EASRRVTGMF PFKVQLMGGV ALHDGNIAEM
110 120 130 140 150
KTGEGKTLTS TLPVYLNALT GKGVHVVTVN EYLASRDAEQ MGKIFEFLGL
160 170 180 190 200
TVGLNLNSMS KDEKREAYAA DITYSTNNEL GFDYLRDNMV LYKEQMVQRP
210 220 230 240 250
LHFAVIDEVD SILIDEARTP LIISGQAAKS TKLYVQANAF VRTLKAEKDY
260 270 280 290 300
TYDIKTKAVQ LTEEGMTKAE KAFGIDNLFD VKHVALNHHI NQALKAHVAM
310 320 330 340 350
QKDVDYVVED GQVVIVDSFT GRLMKGRRYS EGLHQAIEAK EGLEIQNESM
360 370 380 390 400
TLATITFQNY FRMYEKLAGM TGTAKTEEEE FRNIYNMQVV TIPTNRPVVR
410 420 430 440 450
DDRPDLIYRT MEGKFKAVAE DVAQRYMTGQ PVLVGTVAVE TSELISKLLK
460 470 480 490 500
NKGIPHQVLN AKNHEREAQI IEEAGQKGAV TIATNMAGRG TDIKLGEGVK
510 520 530 540 550
ELGGLAVVGT ERHESRRIDN QLRGRSGRQG DPGITQFYLS MEDELMRRFG
560 570 580 590 600
AERTMAMLDR FGMDDSTPIQ SKMVSRAVES SQKRVEGNNF DSRKQLLQYD
610 620 630 640 650
DVLRQQREVI YKQRFEVIDS ENLREIVENM IKSSLERAIA AYTPREELPE
660 670 680 690 700
EWKLDGLVDL INTTYLDEGA LEKSDIFGKE PDEMLELIMD RIITKYNEKE
710 720 730 740 750
EQFGKEQMRE FEKVIVLRAV DSKWMDHIDA MDQLRQGIHL RAYAQTNPLR
760 770 780 790 800
EYQMEGFAMF EHMIESIEDE VAKFVMKAEI ENNLEREEVV QGQTTAHQPQ
810 820 830 840
EGDDNKKAKK APVRKVVDIG RNAPCHCGSG KKYKNCCGRT E
Length:841
Mass (Da):95,531
Last modified:December 1, 1992 - v1
Checksum:i9AAC3630139F5EFF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti126 – 1261V → I in CAA43977 (PubMed:1832735).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10279 Genomic DNA. Translation: BAA01122.1.
U56901 Genomic DNA. Translation: AAC44957.1.
AL009126 Genomic DNA. Translation: CAB15547.1.
X62035 Genomic DNA. Translation: CAA43977.1.
PIRiJQ0647.
RefSeqiNP_391410.1. NC_000964.3.
WP_003228033.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15547; CAB15547; BSU35300.
GeneIDi936711.
KEGGibsu:BSU35300.
PATRICi18979066. VBIBacSub10457_3695.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10279 Genomic DNA. Translation: BAA01122.1.
U56901 Genomic DNA. Translation: AAC44957.1.
AL009126 Genomic DNA. Translation: CAB15547.1.
X62035 Genomic DNA. Translation: CAA43977.1.
PIRiJQ0647.
RefSeqiNP_391410.1. NC_000964.3.
WP_003228033.1. NZ_JNCM01000033.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M6NX-ray2.70A1-802[»]
1M74X-ray3.00A1-802[»]
1TF2X-ray2.90A1-841[»]
1TF5X-ray2.18A1-841[»]
2IBMX-ray3.20A/B1-780[»]
3DL8X-ray7.50A/B1-779[»]
3IQMX-ray3.40A1-802[»]
3IQYX-ray3.30A1-841[»]
3JV2X-ray2.50A/B1-780[»]
5EULX-ray3.70A1-741[»]
A744-780[»]
ProteinModelPortaliP28366.
SMRiP28366. Positions 1-802.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59805N.
IntActiP28366. 2 interactions.
MINTiMINT-8365061.
STRINGi224308.Bsubs1_010100019096.

Proteomic databases

PaxDbiP28366.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15547; CAB15547; BSU35300.
GeneIDi936711.
KEGGibsu:BSU35300.
PATRICi18979066. VBIBacSub10457_3695.

Phylogenomic databases

eggNOGiCOG0653. LUCA.
HOGENOMiHOG000218169.
InParanoidiP28366.
KOiK03070.
OMAiIATERHE.
OrthoDBiEOG654P48.
PhylomeDBiP28366.

Enzyme and pathway databases

BioCyciBSUB:BSU35300-MONOMER.
BRENDAi3.6.3.B1. 658.

Miscellaneous databases

EvolutionaryTraceiP28366.

Family and domain databases

Gene3Di1.10.3060.10. 1 hit.
3.40.50.300. 3 hits.
3.90.1440.10. 1 hit.
HAMAPiMF_01382. SecA.
InterProiIPR027417. P-loop_NTPase.
IPR004027. SEC_C_motif.
IPR000185. SecA.
IPR020937. SecA_CS.
IPR011115. SecA_DEAD.
IPR014018. SecA_motor_DEAD.
IPR011130. SecA_preprotein_X-link_dom.
IPR011116. SecA_Wing/Scaffold.
[Graphical view]
PfamiPF02810. SEC-C. 1 hit.
PF07517. SecA_DEAD. 1 hit.
PF01043. SecA_PP_bind. 1 hit.
PF07516. SecA_SW. 1 hit.
[Graphical view]
PRINTSiPR00906. SECA.
SMARTiSM00957. SecA_DEAD. 1 hit.
SM00958. SecA_PP_bind. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
SSF81767. SSF81767. 1 hit.
SSF81886. SSF81886. 2 hits.
TIGRFAMsiTIGR00963. secA. 1 hit.
PROSITEiPS01312. SECA. 1 hit.
PS51196. SECA_MOTOR_DEAD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing reveals similarity of the wild-type div+ gene of Bacillus subtilis to the Escherichia coli secA gene."
    Sadaie Y., Takamatsu H., Nakamura K., Yamane K.
    Gene 98:101-105(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
  2. "Sequence of the 305 degrees-307 degrees region of the Bacillus subtilis chromosome."
    Soldo B., Lazarevic V., Mauel C., Karamata D.
    Microbiology 142:3079-3088(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  4. "Identification of a gene fragment which codes for the 364 amino-terminal amino acid residues of a SecA homologue from Bacillus subtilis: further evidence for the conservation of the protein export apparatus in Gram-positive and Gram-negative bacteria."
    Overhoff B., Klein M., Spies M., Freudl R.
    Mol. Gen. Genet. 228:417-423(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-364.
  5. "Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA."
    Hunt J.F., Weinkauf S., Henry L., Fak J.J., McNicholas P., Oliver D.B., Deisenhofer J.
    Science 297:2018-2026(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-802 (MONOMERIC AND DIMERIC) WITH AND WITHOUT BOUND ADP.
  6. "A large conformational change of the translocation ATPase SecA."
    Osborne A.R., Clemons W.M. Jr., Rapoport T.A.
    Proc. Natl. Acad. Sci. U.S.A. 101:10937-10942(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF OPEN MONOMERIC SECA.
  7. "A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA."
    Zimmer J., Li W., Rapoport T.A.
    J. Mol. Biol. 364:259-265(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-780 IN A DIMERIC FORM, STUDY OF DIMERIC FORMS, MUTAGENESIS OF GLY-587; ASN-588 AND ARG-750.
  8. "Structure of a complex of the ATPase SecA and the protein-translocation channel."
    Zimmer J., Nam Y., Rapoport T.A.
    Nature 455:936-943(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (7.5 ANGSTROMS) OF 1-779 IN COMPLEX WITH SECYEG FROM A.AEOLICUS.
  9. "Conformational flexibility and peptide interaction of the translocation ATPase SecA."
    Zimmer J., Rapoport T.A.
    J. Mol. Biol. 394:606-612(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-780.

Entry informationi

Entry nameiSECA_BACSU
AccessioniPrimary (citable) accession number: P28366
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: May 11, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.