ID SECA_THEMA Reviewed; 871 AA.
AC Q9X1R4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 145.
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=TM_1578;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN COMPLEX WITH SECYEG.
RX PubMed=18923516; DOI=10.1038/nature07335;
RA Zimmer J., Nam Y., Rapoport T.A.;
RT "Structure of a complex of the ATPase SecA and the protein-translocation
RT channel.";
RL Nature 455:936-943(2008).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-816.
RX PubMed=19850053; DOI=10.1016/j.jmb.2009.10.024;
RA Zimmer J., Rapoport T.A.;
RT "Conformational flexibility and peptide interaction of the translocation
RT ATPase SecA.";
RL J. Mol. Biol. 394:606-612(2009).
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 (By similarity). Part of the essential
CC Sec protein translocation apparatus which comprises SecA, SecYEG and
CC auxiliary proteins SecDF. Other proteins may also be involved. A single
CC SecA monomer interacts with SecY in the channel. {ECO:0000255|HAMAP-
CC Rule:MF_01382, ECO:0000269|PubMed:18923516}.
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; AE000512; AAD36645.1; -; Genomic_DNA.
DR PIR; C72238; C72238.
DR RefSeq; NP_229378.1; NC_000853.1.
DR RefSeq; WP_004082002.1; NZ_CP011107.1.
DR PDB; 3DIN; X-ray; 4.50 A; A/B=1-871.
DR PDB; 3JUX; X-ray; 3.10 A; A=1-816.
DR PDB; 4YS0; X-ray; 1.90 A; A=1-816.
DR PDBsum; 3DIN; -.
DR PDBsum; 3JUX; -.
DR PDBsum; 4YS0; -.
DR AlphaFoldDB; Q9X1R4; -.
DR SMR; Q9X1R4; -.
DR DIP; DIP-59806N; -.
DR IntAct; Q9X1R4; 1.
DR STRING; 243274.TM_1578; -.
DR TCDB; 3.A.5.1.4; the general secretory pathway (sec) family.
DR PaxDb; 243274-THEMA_06390; -.
DR EnsemblBacteria; AAD36645; AAD36645; TM_1578.
DR KEGG; tma:TM1578; -.
DR eggNOG; COG0653; Bacteria.
DR InParanoid; Q9X1R4; -.
DR OrthoDB; 9805579at2; -.
DR BRENDA; 7.4.2.5; 6331.
DR EvolutionaryTrace; Q9X1R4; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
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; IBA:GO_Central.
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 GO; GO:0043952; P:protein transport by the Sec complex; IBA:GO_Central.
DR CDD; cd17928; DEXDc_SecA; 1.
DR CDD; cd18803; SF2_C_secA; 1.
DR Gene3D; 1.10.3060.10; Helical scaffold and wing domains of SecA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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:SF0; CHLOROPLAST PROTEIN-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR30612; SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM; 1.
DR Pfam; PF21090; P-loop_SecA; 2.
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; SSF81886; Helical scaffold and wing domains of SecA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF81767; Pre-protein crosslinking domain of SecA; 1.
DR PROSITE; PS01312; SECA; 1.
DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm;
KW Membrane; Nucleotide-binding; Protein transport; Reference proteome;
KW Translocase; Translocation; Transport.
FT CHAIN 1..871
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000321023"
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"
FT HELIX 6..30
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 33..46
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 57..72
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 126..142
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:4YS0"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:3JUX"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 164..172
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:3JUX"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 209..214
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 254..258
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 276..286
FT /evidence="ECO:0007829|PDB:4YS0"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:4YS0"
FT TURN 299..302
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 329..343
FT /evidence="ECO:0007829|PDB:4YS0"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 350..354
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:4YS0"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:3JUX"
FT HELIX 378..385
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 394..400
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 402..406
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 409..417
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 423..430
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 456..473
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 477..482
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 484..497
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 509..516
FT /evidence="ECO:0007829|PDB:4YS0"
FT TURN 517..520
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 525..529
FT /evidence="ECO:0007829|PDB:4YS0"
FT TURN 530..535
FT /evidence="ECO:0007829|PDB:4YS0"
FT TURN 542..544
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 549..556
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 561..568
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 573..575
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 578..585
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 589..593
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 596..605
FT /evidence="ECO:0007829|PDB:4YS0"
FT STRAND 610..612
FT /evidence="ECO:0007829|PDB:3JUX"
FT HELIX 617..664
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 669..688
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 695..701
FT /evidence="ECO:0007829|PDB:4YS0"
FT TURN 702..704
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 720..742
FT /evidence="ECO:0007829|PDB:4YS0"
FT HELIX 743..745
FT /evidence="ECO:0007829|PDB:3JUX"
FT HELIX 746..778
FT /evidence="ECO:0007829|PDB:4YS0"
FT TURN 780..783
FT /evidence="ECO:0007829|PDB:3JUX"
FT HELIX 786..815
FT /evidence="ECO:0007829|PDB:4YS0"
SQ SEQUENCE 871 AA; 100486 MW; 24F661A1799AC89C 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 SSMLKKKGIP HQVLNAKYHE KEAEIVAKAG QKGMVTIATN MAGRGTDIKL
GPGVAELGGL CIIGTERHES RRIDNQLRGR AGRQGDPGES 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
//
