SECA_TRIEI
ID SECA_TRIEI Reviewed; 936 AA.
AC Q10VW7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=Tery_4635;
OS Trichodesmium erythraeum (strain IMS101).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Microcoleaceae; Trichodesmium.
OX NCBI_TaxID=203124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMS101;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Richardson P.;
RT "Complete sequence of Trichodesmium erythraeum IMS101.";
RL Submitted (JUN-2006) 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 -!- 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}.
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DR EMBL; CP000393; ABG53607.1; -; Genomic_DNA.
DR RefSeq; WP_011613924.1; NC_008312.1.
DR AlphaFoldDB; Q10VW7; -.
DR SMR; Q10VW7; -.
DR STRING; 203124.Tery_4635; -.
DR EnsemblBacteria; ABG53607; ABG53607; Tery_4635.
DR KEGG; ter:Tery_4635; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_3; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
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; Thylakoid; Translocase;
KW Translocation; Transport.
FT CHAIN 1..936
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000318480"
FT BINDING 90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 108..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 499
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 936 AA; 106705 MW; 99F843008ED43780 CRC64;
MFKKLLGDPN ARKLKKFQPW VTDINILEED IQKLSDEELK AKTGEFRQAL EKAKTKDEEK
AILEEILPEA FAVVREAGKR VLSMRHFDVQ LLGGIILHQG QIAEMKTGEG KTLVATLPAY
LNGLTGKGVH VITVNDYLAR RDAEWMGQVH RFLGLSVGLI QQGMNPEERK KNYTCDITYA
TNSEVGFDYL RDNMATNMEE VVQRPFNFCI IDEVDSVLVD EARTPLIISG QVERPSEKYI
KAAEIAAALS KEKEHYEVDE KARNVLLSDE GFAEAEQLLA VQDLYNPEDP WAHFVFNALK
AKELFIKDVN YIVRDDEVVI VDEFTGRVMP GRRWSDGLHQ AIEAKERVDI QPETQTLATI
TYQNFFLLYP KLSGMTGTAK TEEAEFEKIY NLQVTIIPTN KPTGRKDLSD VVYKTEVGKW
KSIAQECAEM HKEGRPVLVG TTSVEKSELL SRLLGEGKIP HQLLNAKPEN VERESEIVAQ
AGRGGAVTIA TNMAGRGTDI ILGGNAEYMA KLKLREYLMP KVVKPEDDDG LGMVRVSGLK
KSHVAKGFDP QQKVKTWKVS PQIFPVKLSQ ETEGMLKLAV NLAVKEWGER ALPELVVEDK
VAIAAEKAPT TEPVIEKLRE VYNLIRQEYE NYIEREHNQV VGCGGLHVIG TERHESRRID
NQLRGRAGRQ GDPGSTRFFL SLEDNLLRIF GGDRVAGMMQ AFGVEEDMPI ESGLLTRSLE
GAQKKVETYY YDMRKQVFEY DEVMNNQRRA IYAERRRVLE GRDLKEQVIK YAEQTMDDIV
EAYINPELPS EEWELDKLVE KVKQFVYLLA DLTPEQLFDL SMEDIRTFMH EQVRNAYDIK
EAQVNQIRGG LMRDAERFFI LQQIDTLWRE HLQQMDALRE SVGLRGYGQK DPLIEYKSEG
YELFLDMMTD IRRNVVYSLF QFQPQPAVQT TAAETV
