ID   SECA_OLILU              Reviewed;         884 AA.
AC   Q32743;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 91.
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};
OS   Olisthodiscus luteus (Marine phytoflagellate).
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Olisthodiscophyceae;
OC   Olisthodiscaceae; Olisthodiscus.
OX   NCBI_TaxID=83000;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Valentin K.-U., Fischer S., Vogel H.;
RT   "Molecular evolution of the sec appartus in plastids.";
RL   Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has a central role in coupling the hydrolysis of ATP to the
CC       transfer of proteins across the thylakoid membrane. {ECO:0000255|HAMAP-
CC       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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000255|HAMAP-
CC       Rule:MF_01382}. Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_01382}; Peripheral membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01382}. Note=A minor fraction is associated
CC       with the chloroplast thylakoid membrane. {ECO:0000255|HAMAP-
CC       Rule:MF_01382}.
CC   -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01382}.
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DR   EMBL; Z35718; CAA84793.1; -; Genomic_DNA.
DR   PIR; S49216; S49216.
DR   AlphaFoldDB; Q32743; -.
DR   SMR; Q32743; -.
DR   PRIDE; Q32743; -.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0009535; C:chloroplast 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; Chloroplast; Membrane; Nucleotide-binding; Plastid;
KW   Protein transport; Thylakoid; Translocase; Translocation; Transport.
FT   CHAIN           1..884
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000109624"
FT   BINDING         82
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         100..104
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   884 AA;  102800 MW;  31C16780AC5B928F CRC64;
     MFNFLENEKY KLKEYQPLVN QINLLETSVK NYTDIELKEQ FDKLRKEYFL SQNFSNDIIA
     RSFSLTREAA FRTIGLRPFD QQLLGGLVLN SGKITEMKTG EGKTLVATLP AALNAISGRG
     VHIVTVNDYL AKRDSTWMGQ IYDYLGLTVG LVQSQMESQE RKDNYFQDIT YITNSELGFD
     YLRDNQVKTF QEMVQRKFNY CIIDEVDAIL IDEARTPLVL SIPDTIHNPK IYLDANTTAK
     SLIRDVDFKA DEKTKNITFT DIGIDKIEYF RKIPNIYGTN AGFLFYLQNA ISANIFFRKN
     SEYIIENNKI AIVDEFTGRV MPVRRWSNGL HEAIEAKESI DITQTSRISS SITYQNFFTL
     YPKLAGMTGT AKSAALELES IYNLEVVVIP TSKKFQRKDL PDKVYTNDFA KWKAIAKECF
     EIHKTGRPIL VGTSSIEKSD FVSFLLENYK LQYNVLNARP ENLKYESEIV GEAGCLNAIT
     IATNMAGRGT DIILGGSPGF KIIRLLKILV LKVKLKEART KKGLFLTHEL YKELQKERLN
     YDAITQLVKF ETEFGQKQIV RQKKLSTLFF YLKINYKSRF KKQKQYINQL GGLYVIGTER
     QDSKRIDNQL RGRAGRQGDA GSSRFFVSIE DKIFRLFGDN KFSNLFNQLN LTNEEISLES
     DLITKTLDNT QERVENYYYD IRKQVYDYDE LITEQRKTFY LFRSKVLKTQ VSGNLIIAST
     EDVIKKIVKS IKTPQLKFTN LTHKQENQII LEDFEQCRRI MRYALPPINL KQINASNHNV
     LFEFLMQEFW ISYDIHKTKA FSSIGEEYYK EYERSCVLES IDHGWSTNLE KMETIRESIV
     WRVYAQKDPL AEYKKEGFST FRKMDEEMKR FLVFAVFDTD FYVT