ID   SECA_SPIOL              Reviewed;        1036 AA.
AC   Q36795;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Protein translocase subunit SecA, chloroplastic {ECO:0000305};
DE            EC=7.4.2.4 {ECO:0000305|PubMed:7629156};
DE   Flags: Precursor;
GN   Name=secA {ECO:0000303|PubMed:7629156};
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=cv. Monatol; TISSUE=Leaf;
RX   PubMed=7629156; DOI=10.1074/jbc.270.31.18341;
RA   Berghoefer J., Karnauchov I., Herrmann R.G., Kloesgen R.B.;
RT   "Isolation and characterization of a cDNA encoding the SecA protein from
RT   spinach chloroplasts. Evidence for azide resistance of Sec-dependent
RT   protein translocation across thylakoid membranes in spinach.";
RL   J. Biol. Chem. 270:18341-18346(1995).
CC   -!- FUNCTION: Has a central role in coupling the hydrolysis of ATP to the
CC       transfer of proteins across the thylakoid membrane.
CC       {ECO:0000305|PubMed:7629156}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + chloroplast-proteinSide 1 = ADP + phosphate +
CC         chloroplast-proteinSide 2.; EC=7.4.2.4;
CC         Evidence={ECO:0000305|PubMed:7629156};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000250|UniProtKB:Q41062}. Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250|UniProtKB:Q41062}; Peripheral membrane protein
CC       {ECO:0000305}. Note=A minor fraction is associated with the chloroplast
CC       thylakoid membrane. {ECO:0000250|UniProtKB:Q41062}.
CC   -!- SIMILARITY: Belongs to the SecA family. {ECO:0000305}.
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DR   EMBL; Z49124; CAA88933.1; -; mRNA.
DR   PIR; A57386; A57386.
DR   AlphaFoldDB; Q36795; -.
DR   SMR; Q36795; -.
DR   OrthoDB; 374850at2759; -.
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-KW.
DR   GO; GO:0016464; F:chloroplast protein-transporting ATPase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017038; P:protein import; IEA:InterPro.
DR   GO; GO:0006605; P:protein targeting; IEA:InterPro.
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   1: Evidence at protein level;
KW   ATP-binding; Chloroplast; Membrane; Nucleotide-binding; Plastid;
KW   Protein transport; Thylakoid; Transit peptide; Translocase; Translocation;
KW   Transport.
FT   TRANSIT         1..?76
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?77..1036
FT                   /note="Protein translocase subunit SecA, chloroplastic"
FT                   /id="PRO_0000031987"
FT   REGION          995..1036
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         186..193
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1036 AA;  116608 MW;  23920878B49A3283 CRC64;
     MESCARSASQ MSSSSCCRCS SFNQKLKQGG IGGGSLPVSF SCVMIGGGGG RRLIDQERGK
     VRGRERKIGE LMQVRASAQG GLLNLGNLLF NFKGGDPAES TKQQYASTVT LINQLEPQIS
     SLTDSQLTDR TSLLRQRALS GESLDSILPE AFAVVREASK RVLGLRPFDV QLIGGMVLHK
     GEIAEMRTGE GKTLVAILPA YLNALTGKGV HVVTVNDYLA RRDCEWVGQV ARFLGLKVGL
     VQQNMTSEVR RENYLCDITY VTNSELGFDF LRDNLATSVD ELVLRGFNFC VIDEVDSILI
     DEARTPLIIS GPAEKPSERY YKAAKIAAAF ERDIHYTVDE KQKTVLIMEQ GYQDAEEILD
     VEDLYDPREQ WALYILNAIK AKELFLKDVN YIIRGKEILI VDEFTGRVMQ GRRWSDGLHQ
     AVEAKEGVPI QNETITLASI SYQNFFLQFP KLCGMTGTAA TESAEFESIY KLKVTIVPTN
     KPMIRKDESD VVFRATSGKW RAVVVEISRM HKTGLPVLVG TTSVEQSESL SEQLQQASIP
     HEVLNAKPEN VEREAEIVAQ SGRLGAVTIA TNMAGRGTDI ILGGNAEFMA RLKIREMLMP
     RVVRPGDGGF VSMKKPPPMK TWKVKETLFP CKLSQKNAKL VDEAVQLAVK TWGQRSLSEL
     EAEERLSYSC EKGPAQDEVI AKLRHAFLEV AKEYKTFTDE EKNKVVLAGG LHVIGTERHE
     SRRIDNQLRG RSGRQGDPGS SRFFLSLEDN IFRVFGGDRI QGLMRAFRVE DLPIESKMLT
     RALDEAQRKV ENYFFDIRKQ LFEYDEVLNS QRDRVYVERR RALESDNLES LLIEYAELTM
     DDILEANIGS DAPKENWDLE KLIAKLQQYC YLLNDLTPEL LSNNCSTYED LQDYLRRCGR
     EAYLQKKDMV ENQAPGLMKE AERFLILSNI DRLWKEHLQA IKFVQQAVGL RGYAQRDPLI
     EYKLEGYNLF LEMMAQIRRN VIYSAYQFKP VVVKNQEQQQ KGKPDSSNVE NKRIGDANLN
     PVSVTESPSS DSPQNT