ID   SECA2_ARATH             Reviewed;        1058 AA.
AC   D8WUA4; F4HY37; Q9XI14;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Protein translocase subunit SECA2, chloroplastic {ECO:0000305};
DE            EC=7.4.2.4 {ECO:0000305|PubMed:21051552};
DE   Flags: Precursor;
GN   Name=SECA2 {ECO:0000303|PubMed:21051552};
GN   OrderedLocusNames=At1g21650 {ECO:0000312|Araport:AT1G21650};
GN   ORFNames=F8K7.6 {ECO:0000312|EMBL:AAD41417.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=21051552; DOI=10.1104/pp.110.166546;
RA   Skalitzky C.A., Martin J.R., Harwood J.H., Beirne J.J., Adamczyk B.J.,
RA   Heck G.R., Cline K., Fernandez D.E.;
RT   "Plastids contain a second sec translocase system with essential
RT   functions.";
RL   Plant Physiol. 155:354-369(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   GENE FAMILY.
RX   PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA   Xu R., Zhang S., Huang J., Zheng C.;
RT   "Genome-wide comparative in silico analysis of the RNA helicase gene family
RT   in Zea mays and Glycine max: a comparison with Arabidopsis and Oryza
RT   sativa.";
RL   PLoS ONE 8:E78982-E78982(2013).
CC   -!- FUNCTION: Involved in protein export. Probably interacts with other
CC       proteins to allow the postimport or conservative sorting pathway for
CC       inner membrane proteins in plastids. May have a central role in
CC       coupling the hydrolysis of ATP to the transfer of proteins across the
CC       membrane. {ECO:0000269|PubMed:21051552}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + chloroplast-proteinSide 1 = ADP + phosphate +
CC         chloroplast-proteinSide 2.; EC=7.4.2.4;
CC         Evidence={ECO:0000305|PubMed:21051552};
CC   -!- SUBUNIT: Part of a second Sec protein translocation apparatus.
CC       Interacts probably with SCY2.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC       {ECO:0000250|UniProtKB:Q41062}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q41062}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=D8WUA4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=D8WUA4-2; Sequence=VSP_042065;
CC   -!- DISRUPTION PHENOTYPE: Embryo lethal. {ECO:0000269|PubMed:21051552}.
CC   -!- MISCELLANEOUS: Cannot substitute for SECA1.
CC   -!- SIMILARITY: Belongs to the SecA family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD41417.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; GU289737; ADI56650.1; -; mRNA.
DR   EMBL; AC007727; AAD41417.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE30132.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30134.1; -; Genomic_DNA.
DR   PIR; E86349; E86349.
DR   RefSeq; NP_001185059.1; NM_001198130.1. [D8WUA4-1]
DR   RefSeq; NP_173584.5; NM_102014.6. [D8WUA4-2]
DR   AlphaFoldDB; D8WUA4; -.
DR   SMR; D8WUA4; -.
DR   STRING; 3702.AT1G21650.3; -.
DR   iPTMnet; D8WUA4; -.
DR   PaxDb; D8WUA4; -.
DR   PRIDE; D8WUA4; -.
DR   ProteomicsDB; 232875; -. [D8WUA4-1]
DR   EnsemblPlants; AT1G21650.1; AT1G21650.1; AT1G21650. [D8WUA4-2]
DR   EnsemblPlants; AT1G21650.2; AT1G21650.2; AT1G21650. [D8WUA4-1]
DR   GeneID; 838767; -.
DR   Gramene; AT1G21650.1; AT1G21650.1; AT1G21650. [D8WUA4-2]
DR   Gramene; AT1G21650.2; AT1G21650.2; AT1G21650. [D8WUA4-1]
DR   KEGG; ath:AT1G21650; -.
DR   Araport; AT1G21650; -.
DR   eggNOG; ENOG502QS62; Eukaryota.
DR   InParanoid; D8WUA4; -.
DR   OMA; SHTIGME; -.
DR   PRO; PR:D8WUA4; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; D8WUA4; baseline and differential.
DR   Genevisible; D8WUA4; AT.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015462; F:ABC-type protein transporter activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016464; F:chloroplast protein-transporting ATPase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017038; P:protein import; IEA:InterPro.
DR   GO; GO:0006605; P:protein targeting; IEA:InterPro.
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   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Chloroplast; Membrane;
KW   Nucleotide-binding; Plastid; Protein transport; Reference proteome;
KW   Transit peptide; Translocase; Translocation; Transport.
FT   TRANSIT         1..58
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           59..1058
FT                   /note="Protein translocase subunit SECA2, chloroplastic"
FT                   /id="PRO_0000414228"
FT   BINDING         167..174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         875..881
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_042065"
SQ   SEQUENCE   1058 AA;  119654 MW;  FB6804C295627030 CRC64;
     MGSVSNLVSP NICHPAPPCL TSRSNKFPWT KPISGLLFYR SVTPIKRCHL VRRSCVVSAS
     LTGNLGRLKR NVQDFTSMNY WVVRDYYRLV ESVNSLEPQI QSLSDEQLKA KTAEFRERLA
     RGESLADMQA EAFAVVREAA KRTIGMRHFD VQIIGGGVLH DGSIAEMKTG EGKTLVSTLA
     AYLNALTGEG VHVVTVNDYL AQRDAEWMGR VHRFLGLSVG LIQRGMKAEE RKFNYSCDIT
     YTNNSELGFD YLRDNLTSNR EQLVMRWPKP FHFAIVDEVD SVLIDEGRNP LLISGEANEN
     AARYPVAAKV AELLVKDSHY KVELKENSVE LTEEGISLAE MALETGDLWD ENDPWARFVM
     NALKAKEFYK RDVQYIVRDG KALIINELTG RVEDKRRWSE GVHQAVEAKE GLEIQADSIV
     VAQITYQSLF KLYPKLSGMT GTAKTEEKEF LKMFQIPVIE VPTNLSNIRI DLPIQAFATA
     RGKWEHVRRE VEDMFGQGRP VLVGTTSVEN SEYLSELLKE WGIPHNVLNA RPKYAAREAD
     FIAQAGRKYA ITISTNMAGR GTDIILGGNP KMLAREIIED SILSYLTSEV LADNIDDDEL
     SQKVLSKIKV GPSSLALLAR ASLMAKYVGK SESKSWTRKK AKSVVTESLE KSQTMDPMEL
     QNLINEQSEM YPLGPAIALA YLSVLKDCEA HCLHEGSEVK RLGGLHVIGT SLHESRRIDN
     QLRGRAGRQG DPGSTRFMIS LQDEMFQKFN FDTEWAVRLI SKITNDEDLP IEGDTIVKQL
     LALQINAEKY FFGIRKSLVE FDEVLEVQRK HVYDLRQLLL TGENESCSQH IFQYMQAVVD
     EIVVGNSNPQ KHPRYWSLAK LLKEFMAISG NLLDESFSGI TEETMLQSLE NLHEGSSIEM
     EDLSLPHLPK PPNAFRGIRR KNSSLRRWLD ICSDNLTGSG SYRTLINLLR KFLGDYLIAS
     YLNVVQESGF DDGYIKEIER AVLLKTLDCY WRDHLVNMNK LSSAVNVRSF AHRNPLEEYK
     IDGCRFFISM LSATRRLTVE SILQYWSSPM ESQELFIS