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Protein

Protein translocase subunit SecA 1

Gene

secA1

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 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 precursor proteins, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane (By similarity).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi101 – 108ATPUniRule annotation8

GO - Molecular functioni

  • ATPase activity Source: MTBBASE
  • ATPase-coupled protein transmembrane transporter activity Source: GO_Central
  • ATP binding Source: MTBBASE

GO - Biological processi

  • evasion or tolerance by symbiont of host-produced reactive oxygen species Source: Reactome
  • growth Source: MTBBASE
  • intracellular protein transmembrane transport Source: UniProtKB-HAMAP
  • protein import Source: InterPro
  • protein targeting Source: UniProtKB-HAMAP
  • protein transport by the Sec complex Source: MTBBASE
Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-7514-MONOMER.
ReactomeiR-HSA-1222387. Tolerance of reactive oxygen produced by macrophages.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein translocase subunit SecA 1UniRule annotation
Short name:
tbSecA
Gene namesi
Name:secA1UniRule annotation
Ordered Locus Names:Rv3240c
ORF Names:MTCY20B11.15c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv3240c.

Subcellular locationi

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

  • Note: Distribution is 50-50.UniRule annotation

GO - Cellular componenti

  • cell envelope Sec protein transport complex Source: MTBBASE
  • cell wall Source: MTBBASE
  • cytosol Source: MTBBASE
  • extracellular region Source: MTBBASE
  • integral component of plasma membrane Source: GO_Central
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001095981 – 949Protein translocase subunit SecA 1Add BLAST949

Proteomic databases

PaxDbiP9WGP5.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi83332.Rv3240c.

Structurei

Secondary structure

1949
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 7Combined sources6
Helixi12 – 26Combined sources15
Helixi28 – 32Combined sources5
Helixi36 – 51Combined sources16
Beta strandi53 – 55Combined sources3
Helixi59 – 78Combined sources20
Helixi84 – 94Combined sources11
Beta strandi97 – 100Combined sources4
Helixi107 – 110Combined sources4
Helixi112 – 119Combined sources8
Beta strandi125 – 131Combined sources7
Helixi132 – 148Combined sources17
Beta strandi153 – 155Combined sources3
Helixi162 – 170Combined sources9
Beta strandi171 – 177Combined sources7
Helixi178 – 188Combined sources11
Helixi194 – 196Combined sources3
Beta strandi204 – 207Combined sources4
Helixi210 – 214Combined sources5
Helixi217 – 219Combined sources3
Beta strandi222 – 227Combined sources6
Helixi232 – 244Combined sources13
Turni247 – 249Combined sources3
Beta strandi250 – 254Combined sources5
Turni255 – 258Combined sources4
Beta strandi259 – 262Combined sources4
Helixi264 – 274Combined sources11
Helixi287 – 300Combined sources14
Turni304 – 306Combined sources3
Beta strandi307 – 309Combined sources3
Beta strandi314 – 317Combined sources4
Beta strandi319 – 321Combined sources3
Helixi334 – 341Combined sources8
Beta strandi350 – 356Combined sources7
Helixi358 – 362Combined sources5
Beta strandi365 – 373Combined sources9
Helixi376 – 378Combined sources3
Helixi379 – 386Combined sources8
Beta strandi389 – 392Combined sources4
Beta strandi407 – 410Combined sources4
Helixi412 – 428Combined sources17
Beta strandi433 – 438Combined sources6
Helixi440 – 452Combined sources13
Beta strandi458 – 460Combined sources3
Helixi465 – 473Combined sources9
Turni474 – 476Combined sources3
Beta strandi481 – 485Combined sources5
Helixi500 – 510Combined sources11
Turni515 – 517Combined sources3
Helixi519 – 536Combined sources18
Helixi539 – 546Combined sources8
Beta strandi549 – 554Combined sources6
Helixi561 – 569Combined sources9
Helixi573 – 575Combined sources3
Beta strandi578 – 585Combined sources8
Helixi589 – 593Combined sources5
Helixi596 – 605Combined sources10
Helixi617 – 663Combined sources47
Helixi669 – 686Combined sources18
Beta strandi689 – 691Combined sources3
Helixi698 – 708Combined sources11
Turni715 – 718Combined sources4
Helixi736 – 758Combined sources23
Helixi762 – 793Combined sources32
Helixi794 – 796Combined sources3
Helixi803 – 832Combined sources30

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NKTX-ray2.60A/B2-892[»]
1NL3X-ray2.80A/B2-892[»]
ProteinModelPortaliP9WGP5.
SMRiP9WGP5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SecA family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CI6. Bacteria.
COG0653. LUCA.
KOiK03070.
OMAiIATERHE.
PhylomeDBiP9WGP5.

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.
IPR000185. SecA.
IPR020937. SecA_CS.
IPR011115. SecA_DEAD.
IPR014018. SecA_motor_DEAD.
IPR011130. SecA_preprotein_X-link_dom.
IPR011116. SecA_Wing/Scaffold.
[Graphical view]
PfamiPF07517. 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. 1 hit.
TIGRFAMsiTIGR00963. secA. 1 hit.
PROSITEiPS01312. SECA. 1 hit.
PS51196. SECA_MOTOR_DEAD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P9WGP5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSKLLRLGE GRMVKRLKKV ADYVGTLSDD VEKLTDAELR AKTDEFKRRL
60 70 80 90 100
ADQKNPETLD DLLPEAFAVA REAAWRVLDQ RPFDVQVMGA AALHLGNVAE
110 120 130 140 150
MKTGEGKTLT CVLPAYLNAL AGNGVHIVTV NDYLAKRDSE WMGRVHRFLG
160 170 180 190 200
LQVGVILATM TPDERRVAYN ADITYGTNNE FGFDYLRDNM AHSLDDLVQR
210 220 230 240 250
GHHYAIVDEV DSILIDEART PLIISGPADG ASNWYTEFAR LAPLMEKDVH
260 270 280 290 300
YEVDLRKRTV GVHEKGVEFV EDQLGIDNLY EAANSPLVSY LNNALKAKEL
310 320 330 340 350
FSRDKDYIVR DGEVLIVDEF TGRVLIGRRY NEGMHQAIEA KEHVEIKAEN
360 370 380 390 400
QTLATITLQN YFRLYDKLAG MTGTAQTEAA ELHEIYKLGV VSIPTNMPMI
410 420 430 440 450
REDQSDLIYK TEEAKYIAVV DDVAERYAKG QPVLIGTTSV ERSEYLSRQF
460 470 480 490 500
TKRRIPHNVL NAKYHEQEAT IIAVAGRRGG VTVATNMAGR GTDIVLGGNV
510 520 530 540 550
DFLTDQRLRE RGLDPVETPE EYEAAWHSEL PIVKEEASKE AKEVIEAGGL
560 570 580 590 600
YVLGTERHES RRIDNQLRGR SGRQGDPGES RFYLSLGDEL MRRFNGAALE
610 620 630 640 650
TLLTRLNLPD DVPIEAKMVT RAIKSAQTQV EQQNFEVRKN VLKYDEVMNQ
660 670 680 690 700
QRKVIYAERR RILEGENLKD QALDMVRDVI TAYVDGATGE GYAEDWDLDA
710 720 730 740 750
LWTALKTLYP VGITADSLTR KDHEFERDDL TREELLEALL KDAERAYAAR
760 770 780 790 800
EAELEEIAGE GAMRQLERNV LLNVIDRKWR EHLYEMDYLK EGIGLRAMAQ
810 820 830 840 850
RDPLVEYQRE GYDMFMAMLD GMKEESVGFL FNVTVEAVPA PPVAPAAEPA
860 870 880 890 900
ELAEFAAAAA AAAQQRSAVD GGARERAPSA LRAKGVASES PALTYSGPAE
910 920 930 940
DGSAQVQRNG GGAHKTPAGV PAGASRRERR EAARRQGRGA KPPKSVKKR
Length:949
Mass (Da):106,022
Last modified:April 16, 2014 - v1
Checksum:iD46C3315835E03D7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP46059.1.
PIRiB70592.
RefSeqiWP_003901576.1. NZ_KK339370.1.
YP_177950.1. NC_000962.3.

Genome annotation databases

EnsemblBacteriaiCCP46059; CCP46059; Rv3240c.
GeneIDi888860.
KEGGimtu:Rv3240c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP46059.1.
PIRiB70592.
RefSeqiWP_003901576.1. NZ_KK339370.1.
YP_177950.1. NC_000962.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NKTX-ray2.60A/B2-892[»]
1NL3X-ray2.80A/B2-892[»]
ProteinModelPortaliP9WGP5.
SMRiP9WGP5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv3240c.

Proteomic databases

PaxDbiP9WGP5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP46059; CCP46059; Rv3240c.
GeneIDi888860.
KEGGimtu:Rv3240c.

Organism-specific databases

TubercuListiRv3240c.

Phylogenomic databases

eggNOGiENOG4105CI6. Bacteria.
COG0653. LUCA.
KOiK03070.
OMAiIATERHE.
PhylomeDBiP9WGP5.

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-7514-MONOMER.
ReactomeiR-HSA-1222387. Tolerance of reactive oxygen produced by macrophages.

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.
IPR000185. SecA.
IPR020937. SecA_CS.
IPR011115. SecA_DEAD.
IPR014018. SecA_motor_DEAD.
IPR011130. SecA_preprotein_X-link_dom.
IPR011116. SecA_Wing/Scaffold.
[Graphical view]
PfamiPF07517. 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. 1 hit.
TIGRFAMsiTIGR00963. secA. 1 hit.
PROSITEiPS01312. SECA. 1 hit.
PS51196. SECA_MOTOR_DEAD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSECA1_MYCTU
AccessioniPrimary (citable) accession number: P9WGP5
Secondary accession number(s): L0TF13
, O05885, P0A5Y8, P71494
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: November 30, 2016
This is version 22 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. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  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.