SECA_THESQ
ID SECA_THESQ Reviewed; 871 AA.
AC B1LB87;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=TRQ2_1241;
OS Thermotoga sp. (strain RQ2).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga;
OC unclassified Thermotoga.
OX NCBI_TaxID=126740;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RQ2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D.B., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga sp. RQ2.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts with
CC the SecYEG preprotein conducting channel. Has a central role in
CC coupling the hydrolysis of ATP to the transfer of proteins into and
CC across the cell membrane, serving as an ATP-driven molecular motor
CC driving the stepwise translocation of polypeptide chains across the
CC membrane. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC cellular proteinSide 2.; EC=7.4.2.8; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01382};
CC -!- SUBUNIT: Monomer and homodimer. Part of the essential Sec protein
CC translocation apparatus which comprises SecA, SecYEG and auxiliary
CC proteins SecDF. Other proteins may also be involved.
CC {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01382}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}.
CC Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-
CC 50. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; CP000969; ACB09585.1; -; Genomic_DNA.
DR RefSeq; WP_012311020.1; NC_010483.1.
DR AlphaFoldDB; B1LB87; -.
DR SMR; B1LB87; -.
DR EnsemblBacteria; ACB09585; ACB09585; TRQ2_1241.
DR KEGG; trq:TRQ2_1241; -.
DR HOGENOM; CLU_005314_3_0_0; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000001687; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0017038; P:protein import; IEA:InterPro.
DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR CDD; cd18803; SF2_C_secA; 1.
DR Gene3D; 3.40.50.300; -; 3.
DR HAMAP; MF_01382; SecA; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000185; SecA.
DR InterPro; IPR020937; SecA_CS.
DR InterPro; IPR011115; SecA_DEAD.
DR InterPro; IPR014018; SecA_motor_DEAD.
DR InterPro; IPR011130; SecA_preprotein_X-link_dom.
DR InterPro; IPR044722; SecA_SF2_C.
DR InterPro; IPR011116; SecA_Wing/Scaffold.
DR InterPro; IPR036266; SecA_Wing/Scaffold_sf.
DR InterPro; IPR036670; SecA_X-link_sf.
DR PANTHER; PTHR30612; PTHR30612; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07517; SecA_DEAD; 1.
DR Pfam; PF01043; SecA_PP_bind; 1.
DR Pfam; PF07516; SecA_SW; 1.
DR PRINTS; PR00906; SECA.
DR SMART; SM00957; SecA_DEAD; 1.
DR SMART; SM00958; SecA_PP_bind; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81767; SSF81767; 1.
DR SUPFAM; SSF81886; SSF81886; 1.
DR PROSITE; PS01312; SECA; 1.
DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm; Membrane;
KW Nucleotide-binding; Protein transport; Translocase; Translocation;
KW Transport.
FT CHAIN 1..871
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000145072"
FT BINDING 80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 98..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 537
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 871 AA; 100498 MW; 355AA1171A4FC98C CRC64;
MILFDKNKRI LKKYAKMVSK INQIESDLRS KKNSELIRLS MVLKEKVNSF EDADEHLFEA
FALVREAARR TLGMRPFDVQ VMGGIALHEG KVAEMKTGEG KTLAATMPIY LNALIGKGVH
LVTVNDYLAR RDALWMGPVY LFLGLRVGVI NSLGKSYEVV WKNPDLARKA IEENWSVWPD
GFNGEVLKEE SMNKEAVEAF QVELKEITRK EAYLCDVTYG TNNEFGFDYL RDNLVLDYND
KVQRGHFYAI VDEADSVLID EARTPLIISG PSKESPSVYR RFAQIAKKFV KDKDFTVDEK
ARTIILTEEG VAKAEKIIGV ENLYDPGNVS LLYHLINALK ALHLFKKDVD YVVMNGEVII
VDEFTGRLLP GRRYSGGLHQ AIEAKEGVPI KEESITYATI TFQNYFRMYE KLAGMTGTAK
TEESEFVQVY GMEVVVIPTH KPMIRKDHDD LVFRTQKEKY EKIVEEIEKR YKKGQPVLVG
TTSIEKSELL SSILKKKGIP HQVLNAKYHE KEAEIVAKAG QKGMVTIATN MAGRGTDIKL
GPGVAELGGL CIIGTERHES RRIDNQLRGR TGRQGDPGES IFFLSLEDDL LRIFGSEQIG
KVMNILKIEE GQPIQHPMLS KLIENIQKKV EGINFSIRKT LMEMDDVLDK QRRAVYSLRD
QILLEKDYDE YLKDIFEDVV STRVEEFCSG KNWDIESLKN SLSFFPAGLF DLDEKQFSSS
EELHDYLFNR LWEEYQRKKQ EIGEDYRKVI RFLMLRIIDD HWRRYLEEVE HVKEAVQLRS
YGQKDPIVEF KKETYYMFDE MMRRINDTIA NYVLRVVKVS EKDEKEAKEE LGKIRLVHEE
FNLVNRAMRR ATEKKKKKDG LHSFGRIRVK R
