SECA_AQUAE
ID SECA_AQUAE Reviewed; 984 AA.
AC O67718;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=aq_1870;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC07677.1; -; Genomic_DNA.
DR PIR; D70461; D70461.
DR RefSeq; NP_214286.1; NC_000918.1.
DR RefSeq; WP_010881222.1; NC_000918.1.
DR AlphaFoldDB; O67718; -.
DR SMR; O67718; -.
DR STRING; 224324.aq_1870; -.
DR PRIDE; O67718; -.
DR EnsemblBacteria; AAC07677; AAC07677; aq_1870.
DR KEGG; aae:aq_1870; -.
DR PATRIC; fig|224324.8.peg.1450; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_0; -.
DR InParanoid; O67718; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015462; F:ABC-type protein transporter activity; IBA:GO_Central.
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; 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; 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 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; Translocase;
KW Translocation; Transport.
FT CHAIN 1..984
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000109574"
FT REGION 930..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..971
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 114..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 595
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 984 AA; 113976 MW; AE23834D330DED84 CRC64;
MLGWIAKKII GTKNEREVKR LRKFVNQINE LEKELDALTN KELVELAQEL HDKIRFDEEL
KERVIKGEIT PEVIKAFALV REAAKRTLGL RHFDVQLIGG LVLHEGKIAE MKTGEGKTLV
ATSPAVVNGM TDEGVHIVTV NDYLARRDAQ WMGPIYKFLG LEVGVINSDG KTYLVEWVDP
EKVKEAIEND VRVWPKGYYE EILPSEKVNI DAKKTYFTTL KEAEHRRKAY EAHITYGTNN
EFGFDYLRDN LAFSKEEIVQ VKGHNYAIVD EVDSILIDEA RTPLIISGPA QIDSQIYHVA
DAVVRKLKKD KDFTVDEKNR TVNLTEQGIK KVEKMLGIDN LYDLKHVDLL HAILQSIRAH
HLFKKDVHYI VRDGEVLIVD EFTGRVLPGR RWSDGLHQAI EVKEGVPVKE ENQTLASITF
QNYFKLYRKL AGMTGTAETE ALEFKEIYGL DVVVIPTHKP MIRKDHPDLV FKTKEEKWER
VVEEVLLNHI FGRPVLVGTV SIEDNEKLSS LLKNKKLLKE IANRNSFKRR LEETAKNLGV
SPEEVQKKLE EVLKKGIPHN VLNAKHHERE AEIIAQAGRV GAVTIATNMA GRGTDILLGG
NPEYLAKQML KEKGINPEEA TEEQFREALR EAYRITEEEK EKVKKLGGLL VIGTERHESR
RIDNQLRGRA GRQGDPGESR FIVSLEDDLL RLFGGERVSK LMDMLKIERG EPIESRMVSK
ALENAQKRVE AQNFQIRKRL YEFDSVMNIQ RDVVYTLRRQ LLEGENVHEK IKEFLKDIIT
QKVNELLPED DPELWDLEPL KAFLKELTGR EVEIPQVRDK EELIQKLYEE LLKIYEEKEK
EIGSPEAMRE LERVILLNLL DNAWREHLHT LDRLREGIYL RGYAGKDPLI EYKREAYELF
ENMMENVKLN TLMTLFNVQI KSEEEIKEVE HEEEKKHQRL LEEAELQGVQ GKSDKKPRPK
TLKERLKEER LRKRKLKAKK KEQE
