ID   SECA_EMIHU              Reviewed;         881 AA.
AC   Q4G377;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 76.
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   Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OG   Plastid; Chloroplast.
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC   Noelaerhabdaceae; Emiliania.
OX   NCBI_TaxID=2903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP373 / CSIRO-CS-57 / BT6;
RX   PubMed=16303746; DOI=10.1093/dnares/12.2.151;
RA   Sanchez-Puerta M.V., Bachvaroff T.R., Delwiche C.F.;
RT   "The complete plastid genome sequence of the haptophyte Emiliania huxleyi:
RT   a comparison to other plastid genomes.";
RL   DNA Res. 12:151-156(2005).
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; AY741371; AAX13889.1; -; Genomic_DNA.
DR   RefSeq; YP_277390.1; NC_007288.1.
DR   AlphaFoldDB; Q4G377; -.
DR   SMR; Q4G377; -.
DR   PRIDE; Q4G377; -.
DR   GeneID; 3562474; -.
DR   Proteomes; UP000013827; Unassembled WGS sequence.
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; Reference proteome; Thylakoid; Translocase;
KW   Translocation; Transport.
FT   CHAIN           1..881
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000318485"
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         492
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   881 AA;  101106 MW;  48D027C0F0028091 CRC64;
     MLEPFFKNYF NQSLTKYNSQ VDAINNFGPM LSNLSDDEIR QRVQILKQQL LSNKNEADII
     CEVFAIVREA TFRTLDIKHF DVQLIGGLVL NDGQIAEMKT GEGKTIVALL PTFLNALYGK
     GVHVVTVNDY LARRDAETVG RVHRFLGLTV GLIQEDMSPE ERKQNYQCDV VYVTNNELGF
     DYLRDNMAFT QEEVVQRPLF YCVVDEVDSI LIDEARTPLI ISGPSEAPTQ KYLQTSQLAR
     VLQKNIHYII DEKNQVVKLT DEGTLFCEQA LKIADLYSPS DPWISYVLNS IKAKELFIRN
     THYIVNVEEE VIIVDEFTGR TMAGRRWSDG LHQAIESKEN LPIQDESQTL ASITYQNLFL
     LYDKLSGMTG TAKTEELEFE KIYGLKVIPI PTHRDVKRKD FPDLVYKNQY LKWQAIANEC
     IKMNEIDRPV LIGTTTIEKS ELLAALLSEY NVPYRLLNAR PENIESEAEI VSQAGCRGAI
     TISTNMAGRG TDIALGGNLE SLLKVKLKKF ISDLVSADFS TVLKSAQFDE FLVSFVPVFE
     TFGLSKLNES SVREDLLEYL NEGIIPDRSD ITDFITAYNS FLKERAAILL EEKTLITKLG
     GLHVIGTERH ESRRIDNQLR GRSGRQGDPG SSRFFLSLDD KLLRLFGGDQ ILNLLQNIGL
     EDDAPIQSPI LTKSLESAQK KVEVYYFDSR KQLFEYDQAL TMQRNGIYSE RKRVLEKESL
     RDWIIEYGER SLYDITLAFS TNTNLALDKF FALKTQELLG MPYQVKWESA KGDINVLLNN
     LKHQFQVSYT LKEAQLEAIE PGIMRELERS FLLQQIDFSW KEHLQKISAL RDSIRWRSYG
     QRDPLTDYKK ESYSTFVTML NRIRHQVIYF IFRSKITIDF E