SECA_THENN
ID SECA_THENN Reviewed; 871 AA.
AC B9K8Q4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=CTN_1161;
OS Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=309803;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E;
RA Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J.,
RA Kim J.J., Park K.J., Lee S.Y.;
RT "The genome sequence of the hyperthermophilic bacterium Thermotoga
RT neapolitana.";
RL Submitted (NOV-2007) 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; CP000916; ACM23337.1; -; Genomic_DNA.
DR RefSeq; WP_015919652.1; NC_011978.1.
DR AlphaFoldDB; B9K8Q4; -.
DR SMR; B9K8Q4; -.
DR STRING; 309803.CTN_1161; -.
DR PRIDE; B9K8Q4; -.
DR EnsemblBacteria; ACM23337; ACM23337; CTN_1161.
DR KEGG; tna:CTN_1161; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_0; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000000445; 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_1000184250"
FT REGION 852..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 100457 MW; AFC6D3839CA83E8D CRC64;
MLFFDKNKRI LKRYSKIVEK INQLDQSMRK KSNEEIVSLS SELKERVNSL EDADRNLVEA
FALVREAARR TLGMRPFDVQ VMGGIALHEG KVAEMKTGEG KTLAATMPVY LNALIGKGVH
VVTVNDYLAR RDALWMGPVY LLLGLRVGVI NSLGKSYEVV WKDPSLVEKA IKENWSVWPQ
EFDGEILKEE QMNKEALNAF QVELKEISRK EAYMCDVTYG TNNEFGFDYL RDNLVLDYND
KVQRGHFYAI VDEADSVLID EARTPLIISG PSKESPSTYR RFAQIAKKFV KDKDFTIDEK
ARTVILTEEG VAKAEKIIGV DNLYEPGNVS LLYHLINALK ALHLFKKDVD YVVMNGEVII
VDEFTGRLLP GRRYSGGLHQ AIEAKEGVPI KEESITYATI TFQNYFRMYE KLAGMTGTAK
TEENEFVQVY GMEVVVIPTH RPMIRKDHDD LVFRTQKEKY EKIVEEIEKR YKKGQPVLVG
TTSIEKSELL SSMLKKKGIP HQVLNAKHHE KEAEIVAKAG QKGMVTIATN MAGRGTDIKL
GPGVAELGGL CVIGTERHES RRIDNQLRGR AGRQGDPGES IFFLSLEDDL LRIFGGEQIG
KVMKILKIEE GQPIQHPMLS KLIENIQKKV EGINFSIRKS LMEMDEVLDK QRSTIYSLRD
QILLEKDYDE YLKQIFEDVI GTRVEEFCSG KNWDLEGLKN SLSFLPRDLF EFDGRRFESS
EELYEYLFNR MWEEYQKKRQ EIGEEYSKVI RFLMLRIIDE HWRRYLEEVE HVREAVQLRA
YGQKDPIVEF KKETYLMFDE MMRRINDTIA NYVLRVVKVT EKDEKEAKEE LGKIRLVHEE
FNLVNRAMRR AMEKGKKKGG SHGLGKIRVK R
