SECA1_ARATH
ID SECA1_ARATH Reviewed; 1022 AA.
AC Q9SYI0;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Protein translocase subunit SECA1, chloroplastic {ECO:0000305};
DE Short=AtcpSecA {ECO:0000303|PubMed:20194926};
DE EC=7.4.2.4 {ECO:0000305|PubMed:21051552};
DE AltName: Full=Protein ALBINO OR GLASSY YELLOW 1 {ECO:0000303|PubMed:20194926};
DE Flags: Precursor;
GN Name=SECA1 {ECO:0000303|PubMed:21051552};
GN Synonyms=AGY1 {ECO:0000303|PubMed:20194926};
GN OrderedLocusNames=At4g01800 {ECO:0000312|Araport:AT4G01800};
GN ORFNames=T7B11.6 {ECO:0000312|EMBL:AAD22642.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 942-1022.
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=20194926; DOI=10.1093/jxb/erq033;
RA Liu D., Gong Q., Ma Y., Li P., Li J., Yang S., Yuan L., Yu Y., Pan D.,
RA Xu F., Wang N.N.;
RT "cpSecA, a thylakoid protein translocase subunit, is essential for
RT photosynthetic development in Arabidopsis.";
RL J. Exp. Bot. 61:1655-1669(2010).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-73, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ALA-72, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [7]
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: Has a central role in coupling the hydrolysis of ATP to the
CC transfer of proteins across the thylakoid membrane. Involved in
CC photosynthetic acclimation and required for chloroplast biogenesis.
CC {ECO:0000269|PubMed:20194926, 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 the Sec protein translocation apparatus. Interacts
CC probably with SCY1.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000250|UniProtKB:Q41062}. Plastid, chloroplast thylakoid membrane
CC {ECO:0000250|UniProtKB:Q41062}; Peripheral membrane protein
CC {ECO:0000305}. Note=A minor fraction is associated with the chloroplast
CC thylakoid membrane. {ECO:0000250|UniProtKB:Q41062}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SYI0-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in green tissues, including cotyledons,
CC rosette and cauline leaves, and sepals. Also detected at the base and
CC the tip of the trichome. {ECO:0000269|PubMed:20194926}.
CC -!- DEVELOPMENTAL STAGE: Induced steadily during photomorphogenesis.
CC {ECO:0000269|PubMed:20194926}.
CC -!- INDUCTION: Up-regulated when light-grown seedlings are shifted to the
CC dark. {ECO:0000269|PubMed:20194926}.
CC -!- DISRUPTION PHENOTYPE: Seedling lethal. Albino seedlings with yellow and
CC translucent (glassy) lateral organs when grown heterotrophically.
CC {ECO:0000269|PubMed:20194926, ECO:0000269|PubMed:21051552}.
CC -!- MISCELLANEOUS: Cannot substitute for SECA2.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD22642.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB77750.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007138; AAD22642.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161492; CAB77750.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82078.1; -; Genomic_DNA.
DR EMBL; BX827284; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; B85023; B85023.
DR RefSeq; NP_192089.1; NM_116410.2. [Q9SYI0-1]
DR AlphaFoldDB; Q9SYI0; -.
DR SMR; Q9SYI0; -.
DR STRING; 3702.AT4G01800.2; -.
DR TCDB; 3.A.5.4.2; the general secretory pathway (sec) family.
DR iPTMnet; Q9SYI0; -.
DR PRIDE; Q9SYI0; -.
DR ProteomicsDB; 232970; -. [Q9SYI0-1]
DR EnsemblPlants; AT4G01800.1; AT4G01800.1; AT4G01800. [Q9SYI0-1]
DR GeneID; 827922; -.
DR Gramene; AT4G01800.1; AT4G01800.1; AT4G01800. [Q9SYI0-1]
DR KEGG; ath:AT4G01800; -.
DR Araport; AT4G01800; -.
DR eggNOG; ENOG502QS7I; Eukaryota.
DR HOGENOM; CLU_005314_3_0_1; -.
DR InParanoid; Q9SYI0; -.
DR PhylomeDB; Q9SYI0; -.
DR PRO; PR:Q9SYI0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SYI0; baseline and differential.
DR Genevisible; Q9SYI0; AT.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0009535; C:chloroplast thylakoid 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 Acetylation; Alternative splicing; ATP-binding; Chloroplast; Membrane;
KW Nucleotide-binding; Plastid; Protein transport; Reference proteome;
KW Thylakoid; Transit peptide; Translocase; Translocation; Transport.
FT TRANSIT 1..72
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 73..1022
FT /note="Protein translocase subunit SECA1, chloroplastic"
FT /id="PRO_0000031985"
FT REGION 985..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176..183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 73
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 1022 AA; 115183 MW; 75D9E80FBFFF5052 CRC64;
MVSPLCDSQL LYHRPSISPT ASQFVIADGI ILRQNRLLSS SSFWGTKFGN TVKLGVSGCS
SCSRKRSTSV NASLGGLLSG IFKGSDNGES TRQQYASIVA SVNRLETEIS ALSDSELRER
TDALKQRAQK GESMDSLLPE AFAVVREASK RVLGLRPFDV QLIGGMVLHK GEIAEMRTGE
GKTLVAILPA YLNALSGKGV HVVTVNDYLA RRDCEWVGQV PRFLGLKVGL IQQNMTPEQR
KENYLCDITY VTNSELGFDY LRDNLATSVE ELVLRDFNYC VIDEVDSILI DEARTPLIIS
GPAEKPSDQY YKAAKIASAF ERDIHYTVDE KQKTVLLTEQ GYEDAEEILD VKDLYDPREQ
WASYVLNAIK AKELFLRDVN YIIRAKEVLI VDEFTGRVMQ GRRWSDGLHQ AVEAKEGLPI
QNESITLASI SYQNFFLQFP KLCGMTGTAS TESAEFESIY KLKVTIVPTN KPMIRKDESD
VVFKAVNGKW RAVVVEISRM HKTGRAVLVG TTSVEQSDEL SQLLREAGIT HEVLNAKPEN
VEREAEIVAQ SGRLGAVTIA TNMAGRGTDI ILGGNAEFMA RLKLREILMP RVVKPTDGVF
VSVKKAPPKR TWKVNEKLFP CKLSNEKAKL AEEAVQSAVE AWGQKSLTEL EAEERLSYSC
EKGPVQDEVI GKLRTAFLAI AKEYKGYTDE ERKKVVEAGG LHVVGTERHE SRRIDNQLRG
RSGRQGDPGS SRFFLSLEDN IFRIFGGDRI QGMMRAFRVE DLPIESKMLT KALDEAQRKV
ENYFFDIRKQ LFEFDEVLNS QRDRVYTERR RALVSDSLEP LIIEYAELTM DDILEANIGP
DTPKESWDFE KLIAKVQQYC YLLNDLTPDL LKSEGSSYEG LQDYLRARGR DAYLQKREIV
EKQSPGLMKD AERFLILSNI DRLWKEHLQA LKFVQQAVGL RGYAQRDPLI EYKLEGYNLF
LEMMAQIRRN VIYSIYQFQP VRVKKDEEKK SQNGKPSKQV DNASEKPKQV GVTDEPSSIA
SA
