SECA_THAPS
ID SECA_THAPS Reviewed; 878 AA.
AC A0T0V8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
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 Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC Thalassiosiraceae; Thalassiosira.
OX NCBI_TaxID=35128;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1335 / NEPCC58 / CCAP 1085/12;
RX PubMed=17252281; DOI=10.1007/s00438-006-0199-4;
RA Oudot-Le Secq M.-P., Grimwood J., Shapiro H., Armbrust E.V., Bowler C.,
RA Green B.R.;
RT "Chloroplast genomes of the diatoms Phaeodactylum tricornutum and
RT Thalassiosira pseudonana: comparison with other plastid genomes of the red
RT lineage.";
RL Mol. Genet. Genomics 277:427-439(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; EF067921; ABK20793.1; -; Genomic_DNA.
DR EMBL; EF067921; ABK20847.1; -; Genomic_DNA.
DR RefSeq; YP_874570.1; NC_008589.1.
DR RefSeq; YP_874624.1; NC_008589.1.
DR AlphaFoldDB; A0T0V8; -.
DR SMR; A0T0V8; -.
DR GeneID; 4524826; -.
DR GeneID; 4524887; -.
DR InParanoid; A0T0V8; -.
DR Proteomes; UP000001449; Chloroplast.
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: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; Reference proteome; Thylakoid; Translocase;
KW Translocation; Transport.
FT CHAIN 1..878
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000318489"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 99..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 878 AA; 101184 MW; FBF07FE57933ACF4 CRC64;
MLKNPFIKDS GLNQYQPLIN QINALETNLK TLTDTELRNK TFELKKRYQE EQDLNALTAE
AFAITREASF RTLGLRHFDV QLIGGLVLNS GKISEMRTGE GKTLVATLPA YLNALTDKGV
HIVTVNDYLA SRDQISMGQI YRFLGLDTGL IQEDMAFLER QQNYKAEITY VTNNEVAFDY
LRDNMASNLS QVVLPPFNYC IVDEVDSIFI DEAQVPLIIS QAVETCIDKY IVAAEVAEYL
EVNVHFKVDE KNRNIILTEQ GTAQIEKILQ VEDLYNPNDP WIPYILSAIK ATALFFRNVH
YIVQNNQIII VDEFTGRIMP DRRWNEGLHQ AVEAKEGVPI RQNTETAASI TYQNFFLLYP
KLSGMTGTAK TSEVEFEKIY NLPVEEIPTA RPNLRKDLPD FVYKDSLTKW TAIARECKSI
ANTKQPILIG TTTVENSEML ADLLQEYQLS YRLLNAKPEN VKRESEIVAQ AGEIGSITIA
TNMAGRGTDI ILGGNTTFKV RKQLYNILVS YKSKTNLTKL NTIFPLAIDI KFTSQKFLSV
LNSLLNDPKF LSLSSTGILK FLNEIDQIRI PKITYQCSIK FLLNELSKFE KKNQTIDNKI
VKNLGGLYII GTERNNSRRI DNQLRGRCGR QGDPGTSRFF LSLEDSLFRN FGSSKLQNFM
QNQLLDDLPL ESNLLTKSLD AAQKRVEERD YDGRKYLFDY DDILNKQRNI VYYERRKLLE
SQSLRETILA YGEQVIKDII TLLKDPKFPK TNSMIEELFK TRLVSLNSDL NSLDSFELKT
YLFQEFWLSY ETKVLEFEIC QTGLIRSFER TIILYYTDIA WKEHLQKIAL LRDAVGWRSY
GQRNPLFEFK EEAYNLFQNR NITIRHLLIR DFLHSFIL
