ID   SECA_PEA                Reviewed;        1011 AA.
AC   Q41062; Q9T2L2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Protein translocase subunit SecA, chloroplastic {ECO:0000305};
DE            EC=7.4.2.4 {ECO:0000269|PubMed:9342223};
DE   Flags: Precursor;
GN   Name=SecA {ECO:0000303|PubMed:9342223};
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=cv. Alaska;
RX   PubMed=7758587; DOI=10.1016/0014-5793(95)00415-6;
RA   Nohara T., Nakai M., Goto A., Endo T.;
RT   "Isolation and characterization of the cDNA for pea chloroplast SecA.
RT   Evolutionary conservation of the bacterial-type SecA-dependent protein
RT   transport within chloroplasts.";
RL   FEBS Lett. 364:305-308(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 279-554, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=7989297; DOI=10.1016/s0021-9258(18)31698-3;
RA   Nakai M., Goto A., Nohara T., Sugita D., Endo T.;
RT   "Identification of the SecA protein homolog in pea chloroplasts and its
RT   possible involvement in thylakoidal protein transport.";
RL   J. Biol. Chem. 269:31338-31341(1994).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=9342223; DOI=10.1111/j.1432-1033.1997.00724.x;
RA   Haward S.R., Napier J.A., Gray J.C.;
RT   "Chloroplast SecA functions as a membrane-associated component of the Sec-
RT   like protein translocase of pea chloroplasts.";
RL   Eur. J. Biochem. 248:724-730(1997).
CC   -!- FUNCTION: Has a central role in coupling the hydrolysis of ATP to the
CC       transfer of proteins across the thylakoid membrane (PubMed:7758587,
CC       PubMed:7989297, PubMed:9342223). Facilitates the transport of precursor
CC       proteins from the chloroplast stroma to thylakoid lumen
CC       (PubMed:7758587, PubMed:7989297, PubMed:9342223).
CC       {ECO:0000269|PubMed:7758587, ECO:0000269|PubMed:7989297,
CC       ECO:0000269|PubMed:9342223}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + chloroplast-proteinSide 1 = ADP + phosphate +
CC         chloroplast-proteinSide 2.; EC=7.4.2.4;
CC         Evidence={ECO:0000269|PubMed:9342223};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000269|PubMed:7989297}. Plastid, chloroplast thylakoid membrane
CC       {ECO:0000269|PubMed:7989297}; Peripheral membrane protein
CC       {ECO:0000305}. Note=A minor fraction is associated with the chloroplast
CC       thylakoid membrane. {ECO:0000269|PubMed:7989297}.
CC   -!- SIMILARITY: Belongs to the SecA family. {ECO:0000305}.
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DR   EMBL; X82404; CAA57798.1; -; mRNA.
DR   PIR; S65668; S65668.
DR   AlphaFoldDB; Q41062; -.
DR   SMR; Q41062; -.
DR   PRIDE; Q41062; -.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0016464; F:chloroplast protein-transporting ATPase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008320; F:protein transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0017038; P:protein import; IEA:InterPro.
DR   GO; GO:0006605; P:protein targeting; IEA:InterPro.
DR   GO; GO:0071806; P:protein transmembrane transport; IDA:UniProtKB.
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..59
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           60..1011
FT                   /note="Protein translocase subunit SecA, chloroplastic"
FT                   /id="PRO_0000031986"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          976..1011
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         164..171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        294
FT                   /note="S -> P (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1011 AA;  114076 MW;  33371D1ADAFFA6C2 CRC64;
     MATSSLCSSF TSQTCNPHSR PHRKTLTLPG SVFLCRQFHL NSPSVSKTRR IRTRQSGPVA
     SLGGLLGGIF KGTDTGEATR KQYAAIVNTI NGLEPKISAL SDSELRDMTF ASRERAQKGE
     SLDSLLPEAF AVVREASKRV LGLRPFDVQL IGGMVLHKGE IAEMRTGEGK TLVAILPAYL
     NALVGKGVHV VTVNDYLARR DCEWVGQVPR FLGMKVGLIQ QNMTSEQKKE NYLCDITYVT
     NSELGFDFLR DNLATSVEEL VIRGFNYCVI DEVDSILIDE ARTPLIISGP AEKSSDQYFK
     AAKIADAFER DIHYTVDEKQ KSVLLSEQGY EDAEEILAVK DLYDPREQWA SFVINAIKAK
     ELFLRDVNYI IRGKEVLIVD EFTGRVMQGR RWSDGLHQAV EAKEGLPIQN ETVTLASISY
     QNFFLQFPKL CGMTGTAATE ITEFESIYKL KVTIVPTNKP MIRKDESDVV FRATTGKWRA
     VVVEISRMNK TGRPVLVGTT SVEQSDSLSQ QLKEAGILHE VLNAKPENVE REAEIVAQSG
     RLGAVTIATN MAGRGTDIIL GGNAEFMARL KLREIMMPRV VKLVAEGEFV SVKKPPPSKT
     WKVNEKLFPC QLSNQNTELA EKAVQLAVKT WGKRSLTELE AEERLSYSCE KGPAQDEVIA
     ELRNAFLEIS KEYKVFTEEE RKKVVAAGGL HVVGTERHES RRIDNQLRGR SGRQGDLGSS
     RFFLSLEDNI FRIFGGDRIQ GLMRAFRVED LPIESQMLTK ALDEAQKKVE NYFFDIRKQL
     FEYDEVLNSQ RDRVYTERRR ALQSVNLQSL LIEYAELTID DILEANIGSD APKESWDLDK
     LIAKIQQYCY LLTDLTPDLL LNECSDYEGL RSYLRLRGKE AYLQKRDIVE QQAPGLMKEA
     ERFLILSNID RLWKEHLQAL KFVQQAVGLR GYAQRDPLIE YKLEGYNLFL EMMAQIRRNV
     IYSIYQFKPV LLKQDQDKME NQKSGKRNAR PPTDTNPDPV GTVEPSTSAS S