ID   SECA_CYACA              Reviewed;         895 AA.
AC   O19911;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 92.
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   Cyanidium caldarium (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX   NCBI_TaxID=2771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RK-1;
RX   PubMed=11040290; DOI=10.1007/s002390010101;
RA   Gloeckner G., Rosenthal A., Valentin K.-U.;
RT   "The structure and gene repertoire of an ancient red algal plastid
RT   genome.";
RL   J. Mol. Evol. 51:382-390(2000).
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; AF022186; AAB82678.1; -; Genomic_DNA.
DR   PIR; T11979; T11979.
DR   RefSeq; NP_045083.1; NC_001840.1.
DR   AlphaFoldDB; O19911; -.
DR   SMR; O19911; -.
DR   PRIDE; O19911; -.
DR   GeneID; 800260; -.
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..895
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000109621"
FT   BINDING         90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         108..112
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         498
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   895 AA;  103754 MW;  DB290CFD201EADBC CRC64;
     MTIYLCIAFN MVNTYIDYLR LRKYWKILNQ IKKHREEIKQ LTNNCLKIKT TEFKKRIKSG
     ISLDQILPET FAVASEAAER VLGLNPYDVQ MIGGIVLHEG KIAEMKTGEG KSLAASFPAY
     LNALTEKGVH IITVNDYLAR RDYESIGKIF EFLGMKVGLI NQYTPISKRK NNYLADITYV
     TNSEIGFDYL RDNMATQIKE LTQRPFHFCI IDEVDSILID ESRTPLIISG RTKTRKDKYE
     LAHRLANFLK KSIHYKIDEK NRTIILSDLG VITCEKILKI KSIYSAQNTW AHFIYNALKA
     KELYLKNVHY IVRDQQAIIV DEFTGRIMPE RRWADGLHQS IEAKENLQIK EETKTLASIT
     YQNLFLLYLK ISGMTGTAKT EENELISIYS LPVICIPTYK SMIRKDLPDL IFQTEIEKLK
     AVTEECVKMH LLGRPILVGT TNIQKSEILS QLLNQYQIRH NLLNAKPQNV KRESEIIAQA
     GRKYAVTIST NMAGRGTDII LGGNLEYIIK NKITSLFKPI ILTGNTQYII IDKSLKSSGN
     EIRDINSNIL KIINLHRQNP KLTIAEFGNS LNIASKKIKS NNEYILNLRS IYIIFENIYK
     KYFDIESKEV KNIGGLCVIG TERHESRRID NQLRGRSGRQ GDVGSSIFFI SLEDNLLRIF
     GGERISKMMH TFMPSVNEPI QSPLLSRSLD SAQKKVESLH YNFRKQLFQY DQILNSQRKA
     IYLERRLILE SNEIVAWTMA YMELTIIDIL NDQYLYSHRK PRDKVLKNIN KIYDLLASPI
     SLIKIEKYTF NKKTILKQLK ISYDLKKAQI DKTSCGLMKS LERSLILEQI DTNWSEHIQQ
     MSFLKEFIGW RGYAQKDPLI EYKNESYILF IKMIRTIRQN ILYLLFRAEP TLDFS