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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)DescriptionActionsGraphical viewLength
Metal bindingi825ZincUniRule annotation1
Metal bindingi827ZincUniRule annotation1
Metal bindingi836ZincUniRule annotation1
Metal bindingi837ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi100 – 107ATPUniRule annotation8

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)DescriptionActionsGraphical viewLength
Mutagenesisi587G → C: Forms position 587-750 dimers upon oxidation in vitro; when associated with C-750. Does not form position 587-587 dimers (homodimers). 1 Publication1
Mutagenesisi588N → C: Forms position 588-588 dimers upon oxidation in vitro (homodimers). 1 Publication1
Mutagenesisi750R → C: Forms position 587-750 dimers upon oxidation in vitro; when associated with C-587. Also forms position 750-750 dimers (homodimers). 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001095761 – 841Protein translocase subunit SecAAdd BLAST841

Proteomic databases

PaxDbiP28366.
PRIDEiP28366.

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 interactors.
MINTiMINT-8365061.
STRINGi224308.Bsubs1_010100019096.

Structurei

Secondary structure

1841
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 6Combined sources6
Beta strandi12 – 14Combined sources3
Helixi18 – 28Combined sources11
Helixi31 – 34Combined sources4
Helixi38 – 53Combined sources16
Helixi58 – 77Combined sources20
Helixi83 – 93Combined sources11
Beta strandi96 – 99Combined sources4
Helixi106 – 118Combined sources13
Turni119 – 122Combined sources4
Beta strandi124 – 130Combined sources7
Helixi131 – 147Combined sources17
Beta strandi152 – 154Combined sources3
Beta strandi157 – 159Combined sources3
Helixi161 – 169Combined sources9
Beta strandi170 – 176Combined sources7
Helixi177 – 187Combined sources11
Helixi193 – 195Combined sources3
Beta strandi203 – 207Combined sources5
Helixi209 – 213Combined sources5
Turni214 – 218Combined sources5
Beta strandi220 – 228Combined sources9
Helixi232 – 241Combined sources10
Turni242 – 244Combined sources3
Beta strandi246 – 250Combined sources5
Beta strandi254 – 256Combined sources3
Beta strandi258 – 261Combined sources4
Helixi263 – 272Combined sources10
Turni275 – 277Combined sources3
Beta strandi278 – 280Combined sources3
Helixi281 – 283Combined sources3
Helixi284 – 298Combined sources15
Turni302 – 304Combined sources3
Beta strandi305 – 309Combined sources5
Beta strandi312 – 316Combined sources5
Turni318 – 320Combined sources3
Helixi330 – 332Combined sources3
Helixi333 – 340Combined sources8
Beta strandi349 – 356Combined sources8
Helixi357 – 361Combined sources5
Beta strandi364 – 372Combined sources9
Helixi375 – 377Combined sources3
Helixi378 – 385Combined sources8
Beta strandi389 – 391Combined sources3
Beta strandi399 – 402Combined sources4
Beta strandi406 – 410Combined sources5
Helixi411 – 427Combined sources17
Beta strandi432 – 437Combined sources6
Helixi439 – 450Combined sources12
Turni451 – 453Combined sources3
Beta strandi457 – 459Combined sources3
Beta strandi461 – 463Combined sources3
Helixi464 – 471Combined sources8
Turni472 – 475Combined sources4
Beta strandi480 – 484Combined sources5
Turni485 – 490Combined sources6
Turni497 – 499Combined sources3
Helixi500 – 502Combined sources3
Beta strandi504 – 511Combined sources8
Helixi516 – 523Combined sources8
Helixi528 – 530Combined sources3
Beta strandi533 – 540Combined sources8
Helixi545 – 547Combined sources3
Helixi550 – 561Combined sources12
Beta strandi565 – 567Combined sources3
Helixi572 – 618Combined sources47
Beta strandi621 – 623Combined sources3
Helixi624 – 641Combined sources18
Beta strandi645 – 648Combined sources4
Helixi649 – 651Combined sources3
Helixi657 – 662Combined sources6
Turni663 – 665Combined sources3
Beta strandi668 – 671Combined sources4
Beta strandi672 – 675Combined sources4
Helixi681 – 702Combined sources22
Turni704 – 706Combined sources3
Helixi707 – 736Combined sources30
Helixi738 – 740Combined sources3
Beta strandi744 – 746Combined sources3
Helixi748 – 776Combined sources29
Beta strandi794 – 797Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28366.

Family & Domainsi

Sequence similaritiesi

Belongs to the SecA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0653. LUCA.
HOGENOMiHOG000218169.
InParanoidiP28366.
KOiK03070.
OMAiIATERHE.
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. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti126V → I in CAA43977 (PubMed:1832735).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP28366.
PRIDEiP28366.

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.
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. 1 hit.
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...

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: November 30, 2016
This is version 151 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.