ID   SECA_TRICV              Reviewed;         888 AA.
AC   P49649;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
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   Trieres chinensis (Marine centric diatom) (Odontella sinensis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta; Mediophyceae;
OC   Biddulphiophycidae; Eupodiscales; Parodontellaceae; Trieres.
OX   NCBI_TaxID=1514140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kowallik K.V., Stoebe B., Schaffran I., Kroth-Pancic P., Freier U.;
RT   "The chloroplast genome of a chlorophyll a+c-containing alga, Odontella
RT   sinensis.";
RL   Plant Mol. Biol. Rep. 13:336-342(1995).
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; Z67753; CAA91661.1; -; Genomic_DNA.
DR   PIR; S78288; S78288.
DR   AlphaFoldDB; P49649; -.
DR   SMR; P49649; -.
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..888
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000109623"
FT   BINDING         81
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         99..103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         489
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   888 AA;  102946 MW;  1ACF715ADB5C5097 CRC64;
     MLKNPFKKKS IADKYQTLIR EINALESTVK TLTDGELRNK TNQLKQRYQD EQNLNNLIVE
     SFALTREASY RTLGLRHFDV QLIGGLVLNG GKIAEMRTGE GKTLVATLPA YLNALTKKGV
     HIVTVNEYLA SRDQTSMGQI YRFLGLETGL IQEKMTTPER QRNYKADITY VTNNELGFDY
     LRDNLALNIR DVFLRPFNYC IVDEVDSVLI DEALTPLIIA NSVKTCVDKY IIASEITDYL
     ELNVHFEIDE KNKSVLLTNQ GTIQIEKILG VQDLYNPRDP WIPYVINAIR ASSLFFRDVH
     YIVQNNRIVI VDEFTGRIMP DRRWRHGLHQ AVEAKENVAI RQTTEITASI TYQNFFLVYP
     KLSGMTGTAK TAEVEFDKIY SLPVEEIPTA RPNLRQDLPD LIYKDEFSKW NAIAKECQNI
     SLVKQPILIG TTTVEKSEML AQLLQEYRLS HQILNAKPEN VRRESEIVAQ AGKKGSITIA
     TNMAGRGTDI ILGGNIQFKV RKDLYNILVT YKYQTKENKK DSLSRSLQIF PLLKKLQRTS
     QKFLTVLNCL INNKQFLNLS DVEVLKILNE SELIRVPKIS YQCSMKFLIN ELVNFEKKTQ
     KLDNVIVKNL GGLYIIGTER NDSQRIDNQL RGRCGRQGDP GKSRFFLSVE DKLIRLFGDA
     RLENVLKSQL LDDLPLESEL VTKILDSAQK RVEERNYELR KNLFDYDDIL NKQRNVVYYE
     RRKVLESESA RIKILAYGEQ VISEITSKLR RKKVFGSQLI SRIRNLLGTK FLLNFPSSDL
     NNLESIDFQT YLLQEFWLSY ESKILELEVE YPGIIQEFER TLILIYMDRE WKEHLQKMSL
     LRDAVGWRKY GQRNPLSEYK EDAYKLFKYR GIVTRHLVIY ELLRSSIL