SECA_THEVB
ID SECA_THEVB Reviewed; 929 AA.
AC Q8DHU4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=tll1851;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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 -!- FUNCTION: Probably participates in protein translocation into and
CC across both the cytoplasmic and thylakoid membranes in cyanobacterial
CC cells. {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 Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01382};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01382};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}. Cytoplasm
CC {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000039; BAC09403.1; -; Genomic_DNA.
DR RefSeq; NP_682641.1; NC_004113.1.
DR RefSeq; WP_011057688.1; NC_004113.1.
DR AlphaFoldDB; Q8DHU4; -.
DR SMR; Q8DHU4; -.
DR STRING; 197221.22295577; -.
DR EnsemblBacteria; BAC09403; BAC09403; BAC09403.
DR KEGG; tel:tll1851; -.
DR PATRIC; fig|197221.4.peg.1934; -.
DR eggNOG; COG0653; Bacteria.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid 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; -; 2.
DR HAMAP; MF_01382; SecA; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
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; 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 TIGRFAMs; TIGR00963; secA; 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; Reference proteome; Thylakoid;
KW Translocase; Translocation; Transport.
FT CHAIN 1..929
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000318466"
FT BINDING 83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 101..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 491
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 929 AA; 105848 MW; 59341DBCAFC94D72 CRC64;
MLKALFGDPN QRKVKKYQPL VVEINLLEEQ VQALSDSELQ AKTAEFRQRL DNGETLDDLL
PEAFAVVREA SRRVLGMRHF DVQLIGGMIL HDGQIAEMKT GEGKTLVATL PAYLNALTGK
GVHIVTVNDY LARRDAEWMG QVHRFLGLTV GLIQQQMAPQ ERQKSYACDI TYATNSEIGF
DYLRDNMATS MVEVVQRPFN YCIIDEVDSV LIDEARTPLI ISGQVERPTE KYLKAAEIAR
LLKKDEHYEV DEKARNVLMT DEGFIEAEKL LGVSDLYDPQ DPWAHYIFNA IKAKELFQRD
VNYIVRNGEV VIVDEFTGRV MVGRRWSDGL HQAIEAKEGL EIQNESQTLA TITYQNLFLL
YPKLAGMTGT AKTEEAEFEK IYKLEVTVVP TNRPSQRRDF PDVVYKTERA KWLAVASECA
EVHATGRPVL VGTTSVEKSE LLSQLLRELE IPHNLLNAKP ENVEREAEII AQAGRKGAVT
ISTNMAGRGT DIILGGNADY MARLKVREYF MPRIVMPPSD DPMMLLGLKM DRGGGQGFSQ
GAQKNWKASP GLFPCEMSKE AEKLLRHAVD VAVKTYGERS LPELQAEDML AIASEKAPTE
DPVIQALRDA FNRIREEYEV VTKKEHEEVV ALGGLHVIGT ERHESRRIDN QLRGRAGRQG
DPGSTRFFLS LEDNLLRIFG GDRIASIMNA MRIDEDMPIE SPLLTRSLEN AQRKVETYYY
DIRKQVFEYD EVMNNQRRAI YAERRRVLEG EDLKDRVLEY AEKTMDDIIA AYVNPDLPPE
EWDLEGLVAK VQEFVYLLAD LRPEHLAHLS VPEMQAFLHE QVRTAYEQKE AQIEAIQPGL
MRQAERFFIL QQIDLLWREH LQQMDALRES VGLRGYGQED PLVEYKREGY ELFLDMMVMI
RRNVVYSLFQ FQPQVAPPPE QVSSSSEQG
