ID   SECA_RHDSA              Reviewed;         877 AA.
AC   A6MVS6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 62.
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   Rhodomonas salina (Cryptomonas salina).
OG   Plastid; Chloroplast.
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Pyrenomonadaceae; Rhodomonas.
OX   NCBI_TaxID=52970;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1319 / NEPCC76 / CS-174;
RX   PubMed=17522086; DOI=10.1093/molbev/msm101;
RA   Khan H., Parks N., Kozera C., Curtis B.A., Parsons B.J., Bowman S.,
RA   Archibald J.M.;
RT   "Plastid genome sequence of the cryptophyte alga Rhodomonas salina
RT   CCMP1319: lateral transfer of putative DNA replication machinery and a test
RT   of chromist plastid phylogeny.";
RL   Mol. Biol. Evol. 24:1832-1842(2007).
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; EF508371; ABO70845.1; -; Genomic_DNA.
DR   RefSeq; YP_001293505.1; NC_009573.1.
DR   AlphaFoldDB; A6MVS6; -.
DR   SMR; A6MVS6; -.
DR   GeneID; 5228615; -.
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..877
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000318484"
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         491
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   877 AA;  100330 MW;  425FF3992DBE04F0 CRC64;
     MLQILFGDPN ERKIGRYKQI VNRINALEEE FKQLTDKELQ NRTAIFISDI SKNADLDNVL
     PSAFAVAREA SFRVLGLRHF DVQLIGGMIL HEGKIAEMKT GEGKTLVAIL PAYLNALCGY
     GVHIVTVNDY LARRDAEWVG QVPKFLGLSV GLIQEGMTQE ERKNNYSQDI TYTTNSELGF
     DYLRDNMAIL LQDIVQRPFY FCIIDEVDSI LIDEARTPLI ISGAGETTEE KYVQASKVSL
     NLVKNLHYEV DEKARNILLT DSGIVESEKQ LECKDLYNVQ NPWASYIFNA LKAKELFIKD
     VHYIVKDSEV IIVDEFTGRI MQGRRWSDGL HQAIEAKENV PTQNETQTLA SITYQNFFLL
     YPKLSGMTGT AKTEEAELDK IYALEVTCVP THRPMQRKDY SDLIYKNQYA KWKSIADECL
     DMHTLGRPVL IGTTSVEKSE LLSSLLKEYG VPHNLLNAKP ENIKREAEII AQAGRKGAVT
     IATNMAGRGT DILLGGNSNY MAKNALNILL KEVPSKSSFT KNDPQLQSLH SFLLNKIESY
     EIDDDELETK ISIACEKGFT EDALTITLRA AYQILIEKYS SLIKKEQGEV IALGGLHVIG
     TERHESRRVD NQLRGRAGRQ GDPGSSRFFL SLEDNLLRIF GGDKIVNLME TLRVEEDVPI
     ESMLLNKSLE SAQKKVEAYY YDARKQLFEY DEVLNYQRLA IYSERRRILE SNNLRDWVIQ
     YAETTIEDYI EHYFDKKHSM PNSASEVLDK IEDLLGLPYD LDPMYFETLS TSEAKNFLYQ
     QVRIAYDLKE SQIDLIENGL MRELERSFLL QKIDSAWKEH LQQMNSLRES IGWRGYGQKD
     PLIEYKNEAY DLFTSMTTNI RHSVVYLIFR SQPILKN