ID   SECA_DIALT              Reviewed;         891 AA.
AC   Q01570;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 101.
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   Diacronema lutheri (Unicellular marine alga) (Monochrysis lutheri).
OG   Plastid; Chloroplast.
OC   Eukaryota; Haptista; Haptophyta; Pavlovales; Pavlovaceae; Diacronema.
OX   NCBI_TaxID=2081491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1423730; DOI=10.1007/bf00352444;
RA   Scaramuzzi C.D., Hiller R.G., Stokes H.W.;
RT   "Identification of a chloroplast-encoded secA gene homologue in a
RT   chromophytic alga: possible role in chloroplast protein translocation.";
RL   Curr. Genet. 22:421-427(1992).
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; X65961; CAA46776.1; -; Genomic_DNA.
DR   PIR; S27029; S27029.
DR   AlphaFoldDB; Q01570; -.
DR   SMR; Q01570; -.
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..891
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000109625"
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         489
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   891 AA;  102028 MW;  97CA1A069A2FAF98 CRC64;
     MLKDILRKTT QSDLYRYENI VKKINDLERV MKPLTNEELR AKTLGFRKSI EDGQSIDNIL
     PEAFGLVREA SLRILGLRHY DVQLIGGCIL HDSKIAEMKT GEGKTLVAIL PAYLNALSGK
     SVHIVTVNEY LAKRDSLSVG RVLSFLGLSV GLILADMNRE ERQENYKCDV IYTTNSELGF
     DYLRDNLVGN PSEKVQNGFE FAIIDEVDSV LIDEARTPLI ISRSLETLNN IYLTAKNVAQ
     AFEINTHYEI DKRNRNVYLN ESGSKLAEKL LGVSSIYKFE TGTYILNAIK AKEFYTKDKD
     YLVMRNQITI VDEFTGRILK GRRWGDGLHQ AIEAKEGVTV GSETMTMASI TYQNFFLFYK
     KLSGMTGTAL TEAKEFKKIY NLSVDCVPIN KKVNRIDKED VVYKSLYAKW KAVLYESLSI
     HEQGRPLLIG TSNVKNSEIV SGLLKEYNIK HSLLNAKPEN AANESEIIAQ AGRKGSVTIA
     TNMAGRGTDI LLGGNPDFLT KGELRYIFRS IVLSLDDMTV PKNELINNLK YKYVISEKNR
     LDVEELIDKL KSAYTVPEKN RIGVEELIEN IDESFQPVDK FEILIQKLYE KTKERYVREC
     LAEKEEVIQL GGLHIIGTEK HDSRRIDNQL RGRAGRQGDP GSSKFFLSFE DRLIEIFTTG
     GLKNMIKELD LEDDQPVEGK IVSLSIESAQ KRIEDKNYQV RKQLFNYDNV LNLQRKVIYD
     ERDRFLSLTD FKGLILQYLE KLVDDVVAEM ERSENQEDKS RGIVLFCKKF ICLPYSIDPE
     LLSNLSKEEI KIFLNDQVKI SYELKEIELE SLRVGLSQSL EYAFLLQSID QVWKEQLTRM
     ELLKESIGWR AYGQRDPLLE YQKEAYRIFA IQTRKIRHSA SHLIMCSTSF A