ID   SECA_PORPU              Reviewed;         884 AA.
AC   P51381;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
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   Porphyra purpurea (Red seaweed) (Ulva purpurea).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX   NCBI_TaxID=2787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Avonport;
RA   Reith M.E., Munholland J.;
RT   "Complete nucleotide sequence of the Porphyra purpurea chloroplast
RT   genome.";
RL   Plant Mol. Biol. Rep. 13:333-335(1995).
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; U38804; AAC08267.1; -; Genomic_DNA.
DR   PIR; S73302; S73302.
DR   RefSeq; NP_053991.1; NC_000925.1.
DR   AlphaFoldDB; P51381; -.
DR   SMR; P51381; -.
DR   GeneID; 810020; -.
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..884
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000109626"
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   884 AA;  101326 MW;  A415846D12B90B2B CRC64;
     MFNLLFSSSN QRRINSYAAT VKKINSLEQK IGNLSDEELF TKTSYFKDEL KKGVTLDYIL
     PEAFSVVREA GCRVLGLRVF DVQIIGAIIL HQGKIAEMKT GEGKTLVATL AGYLNALSGK
     GVHIVTVNDY LARRDSEWVG QIHKFLGLSV GLIQQDLSKA ERKLAYQCDV TYVTNSELGF
     DYLKDNMVLS MSEIVQNKFA FCIIDEVDSI LIDEARTPLI ISGPSEAPVE KYTQTNLLSN
     ILFKDVHYEV DEKARNIILT DKGTLFCEDH LSIDNLYDLE NPWVHYILNA IKAKELFIKD
     VHYIIRDNQV VIVDEFTGRI MSGRRWSDGL HQAIEAKEQV PIQQENQTYA SITYQNFFLL
     YPKLSGMTGT AKTEESELDK IYNLEVICVP THRPLRRKEF SDLVYSNEYR KWEAIADECY
     DMYRAGRPTL VGTTSVEKSE LLSKLLTEYK IPHSLLNAKP ENVEKESDII AQAGRQSSVT
     IATNMAGRGT DIILGGNPSY IAKSILIDLL IKKISVQNNL KLQQLSLKTQ YCINQILKSL
     EDDLIYANLS VLELEKKISI ACEQVAISRN LEIQLRKAYQ LIFQEYENIF SQEKKYVAQA
     GGLHVIGTER HESRRIDNQL RGRAGRQGDP GSSRFFLSIE DNLLRIFGGN KIADLMQALN
     VDDDTPMEST LLSKSLEAAQ KKVEAYFYDT RKQVFEYDQV LNSQRQAIYA ERRRILESGY
     PRDCILQYAE STIDDIVNFC LTSKENNEKF VNLNTKIKYL LNATDTFFIS KDLYSDSSEL
     KKWITEQVRI NYDLREAYLE QIKPGLIRQL EKYYLLQQID NAWKDHLQKM GALRDAIGWR
     SYGQQDPLVE YKNEAFNLFI EMITHVKHTV VYAILRSRLM VKND