ID   SECA_GRATL              Reviewed;         882 AA.
AC   Q6B8L3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
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}; OrderedLocusNames=Grc000191;
OS   Gracilaria tenuistipitata var. liui (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC   Gracilariaceae; Agarophyton; Agarophyton tenuistipitatum.
OX   NCBI_TaxID=285951;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15638458; DOI=10.1007/s00239-004-2638-3;
RA   Hagopian J.C., Reis M., Kitajima J.P., Bhattacharya D., de Oliveira M.C.;
RT   "Comparative analysis of the complete plastid genome sequence of the red
RT   alga Gracilaria tenuistipitata var. liui provides insights into the
RT   evolution of rhodoplasts and their relationship to other plastids.";
RL   J. Mol. Evol. 59:464-477(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY673996; AAT79772.1; -; Genomic_DNA.
DR   RefSeq; YP_063697.1; NC_006137.1.
DR   AlphaFoldDB; Q6B8L3; -.
DR   SMR; Q6B8L3; -.
DR   PRIDE; Q6B8L3; -.
DR   GeneID; 2944148; -.
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..882
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000318487"
FT   BINDING         79
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         97..101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         487
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   882 AA;  103025 MW;  53BAA78BCF1CCC54 CRC64;
     MFNFFKKNKL NKFQNTINEI HQIGNTVKNY SDAELKKQTH KLKKKIIQNS NLTEILPESF
     AIVKEAIKRS TGMILFDVQL VGSIVLHQGQ IAEMKTGEGK TIVAITTGYL NALTSKGVHI
     ITVNDYLAKR DSELAQKICS YIDLKVGLIT QSMTYEEKKR AYDCDITYIT NSELGFDYLR
     DNMAIEFNQI VQRGFNFAII DEVDSILIDE ARTPLIISGP FEIEINKYKK STSIANTLQK
     DLDYEIDEKT KNITLTEKGI SRCENMLNID NLYDIHDSWI QYLLNSLKAK DLFLKNQHYI
     VKNNEIIIVD EFTGRVMQGR RWSDGLHQAI ESKENIPIQQ ENKTLASITY QNLFLLYEKL
     SGMTGTAKTE ETELDKIYNL EVLEIPTNKI CKRQDLPDLV YKTEYKKWQA IADECFDMYH
     IGRPTLIGTT NVEKSELLAK ILMELQIPFN LLNAKPENVS REAEIITQAG RKNTITISTN
     MAGRGTDIIL GGNPEALSKL ALTYYLQNKL GLKVNYLLNN IETQITTIIN NYVLDMQELD
     IYKYKNIDLK KIQYYIEKII KNEHTKYSEE EKLQKLYLKI LSEYKNICYQ EKQEVLKLGG
     LYVIGTERHE SRRIDNQLRG RAGRQGDIGA SRFFLSLEDN LLRIFGGDKI SQLMDNLNID
     EHTPIESIIL SKSLDSAQKK VESYFYDIRK QLFEYDEVIN NQRQAIYAER KRILQSSFTR
     DCIIEYAEST IDEILTAFYR EDNINNKNHI IKKIYQLLNL TENFHFNTLY DMNYKQIQEF
     LYEQLRISYD LRESYLEQLR PGLIRKLEKY YLLQQIDKAW QDHLDKMALL RESIGWRSYG
     QQDPLVEYKN EAFSLFINMV RYIRQTVTYL TMRSRLIINV NN