SECA_GUITH
ID SECA_GUITH Reviewed; 877 AA.
AC O78441;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
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 Guillardia theta (Cryptophyte) (Cryptomonas phi).
OG Plastid; Chloroplast.
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX NCBI_TaxID=55529;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9929392; DOI=10.1007/pl00006462;
RA Douglas S.E., Penny S.L.;
RT "The plastid genome of the cryptophyte alga, Guillardia theta: complete
RT sequence and conserved synteny groups confirm its common ancestry with red
RT algae.";
RL J. Mol. Evol. 48:236-244(1999).
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; AF041468; AAC35626.1; -; Genomic_DNA.
DR RefSeq; NP_050692.1; NC_000926.1.
DR AlphaFoldDB; O78441; -.
DR SMR; O78441; -.
DR PRIDE; O78441; -.
DR GeneID; 856984; -.
DR HOGENOM; CLU_005314_3_2_1; -.
DR OMA; SHTIGME; -.
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..877
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000109622"
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 877 AA; 100567 MW; 99240D78BA543580 CRC64;
MLNVLFGDPN ERRINPYKQI VNKINYLEAK LKKLTDSELQ EQTERFIKLL SNNSSNEELL
PEIYATVREA SLRVLGLRHF DVQLIGGLIL NDGKIAEMKT GEGKTLVALL PTYLNALAGF
GVHVVTVNDY LARRDSEWVG QVHKFLGLTV GLIQEGMSQF ERRENYLKDV TYATNSELGF
DYLRDNMAID LEDIVQRPFY FCVIDEVDSI LIDEARTPLI ISGPGNSPVN KYIKANVISQ
DLIKDIDYEI DEKARNVILT DNGILKCENL LGNTDIFNLQ DPWAPYIFNA IKAKELFLEN
IHYIIRNQEI VIVDEFTGRI MSGRRWSDGL HQAIEAKESV PIQSETQTLA SITYQNFFLL
YPKLSGMTGT AKTEETELDR IYGLEVNCVP THKIMQRVDF PDLIYKTQYS KWKSIADECL
DMHNLGRPVL IGTTSVEKSE LLSSLLKEYG VPHNLLNAKP ENVQREAEIV AQAGRLGAVT
IATNMAGRGT DILLGGNTSY MARTALIDLL HVNDASTIST DIATNVDFLK LKTFIQTKLD
IETFINDPQC NLKLGLACEK SFTNDEQIIT LRAVYQVLIE YYEKLLSPEK LRVQSLGGLH
VIGTERHESR RIDNQLRGRA GRQGDPGSSR FFLSLDDNLL RIFNGDKIAK IMDQLQIDED
LPIESKLLNS SLESAQKKVE AYYYDARKQL FDYDEVLNYQ RQAIYFERRK ILETNNLRSW
ILQYAETTIE QYIEDYFSKE ANNLEACLAN IEFLLGLNNF FDVIYCSTLN RNDLKQFIIQ
QLYIAYDLKE SQIDLIETGL MRELERSFLL QKIDSSWKEH LQQITILRES IGWRGYGQKD
PLIEYKNEAF NLFVNMVSKI RQSVVYLVFR SQPILKN
