ID   SECA_ANTSP              Reviewed;         878 AA.
AC   Q06461;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 98.
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   Antithamnion sp. (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Ceramiales;
OC   Ceramiaceae; Antithamnion; unclassified Antithamnion.
OX   NCBI_TaxID=2767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8437571; DOI=10.1007/bf00277119;
RA   Valentin K.-U.;
RT   "SecA is plastid-encoded in a red alga: implications for the evolution of
RT   plastid genomes and the thylakoid protein import apparatus.";
RL   Mol. Gen. Genet. 236:245-250(1993).
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; X64705; CAA45961.1; -; Genomic_DNA.
DR   PIR; S42707; S42707.
DR   AlphaFoldDB; Q06461; -.
DR   SMR; Q06461; -.
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..878
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000109620"
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   878 AA;  102179 MW;  E6275F17551E9EC6 CRC64;
     MFNFLFSNKI NQYQRIVKQI NSLDSTYNKY SDQELKQQTN KLKDQIIATQ DIDTILPKAF
     AITKEAIKRA TGLLLFDVQL IGAIILNQGK IAEMKTGEGK TLVAMLTAYL NSLFNKGVHI
     VTVNEYLAKR DATLAKQIFE YLNIHIGIID QSMHSQERKK QYSCDITYLT NSELGFDYLR
     DNMAIQKEDL VQRDFFFAII DEIDSILIDE ARTPLIISGP ANNKLTEYLE ANKVANLLNQ
     NTDYEIDEKN KNIILNENGI KKSENILDIN NLYDIQKPWI KYILNALKAK EIFIKNKDYI
     VKNNEIVIVD EFTGRIMEGR RWSDGLHQAI EAKEKQKIQQ ENKTLASITY QNLFLLYEKL
     SGMTGTAKTE EAELEQIYKL KVVEIPTNKL NQRKDLSDLV YKTEYVKWKA VANECFDMYQ
     IGRPTLVGTT SIEKSELLAK ILKELQVPYN LLNRKPENIT RESEIITQAG RKYTITISTN
     MAGRGTDIIL GGNPQILAKT ALTIHINKIL NLTQYNTNYK IENEITYILN SINNTLLINN
     IDINSQDISQ SINNIINNNM IQDAKSYKIS NIYKIVLNKY KQLCHNEKQE IITLGGLYVI
     GTERHESRRI DNQLRGRSGR QGDLRSSRFF LSLQDNLLKI FGGDKISDFM QNLNIDEDMP
     IESSILNKSL SSAQKKIEAY FYDVRKQLFE YDEVLNNQRQ AIYIERKRLL KSNYTRDCIL
     EYAESTIEEM LVTYNQQTDI SEKTKILSKI LKLLNLNIYI NNNILLNMEE NDIKSFLFEQ
     LRITYDLRES YLEQLRPGLI RQLEKYYLLQ QIDYAWQEHI NKISILKESI GWRSYGQQDP
     LIEYKNEAFN LFINMVTYIR QTVIYLTMRS RLIVNIDN