SECA_PHATC
ID SECA_PHATC Reviewed; 886 AA.
AC A0T0G5; Q5D709;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
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 Phaeodactylum tricornutum (strain CCAP 1055/1).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC Phaeodactylum.
OX NCBI_TaxID=556484;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1055/1;
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; EF067920; ABK20663.1; -; Genomic_DNA.
DR RefSeq; YP_874440.1; NC_008588.1.
DR AlphaFoldDB; A0T0G5; -.
DR SMR; A0T0G5; -.
DR STRING; 556484.A0T0G5; -.
DR PRIDE; A0T0G5; -.
DR GeneID; 4524563; -.
DR InParanoid; A0T0G5; -.
DR Proteomes; UP000000759; 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: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; Reference proteome; Thylakoid; Translocase;
KW Translocation; Transport.
FT CHAIN 1..886
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000318488"
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"
FT VARIANT 35
FT /note="S -> G (in strain: UTEX 646 / Bohlin)"
FT VARIANT 152..153
FT /note="QD -> HE (in strain: UTEX 646 / Bohlin)"
FT VARIANT 183
FT /note="D -> G (in strain: UTEX 646 / Bohlin)"
FT VARIANT 211
FT /note="D -> G (in strain: UTEX 646 / Bohlin)"
FT VARIANT 374
FT /note="T -> A (in strain: UTEX 646 / Bohlin)"
SQ SEQUENCE 886 AA; 102221 MW; 62C9BFBB06CE129E CRC64;
MLKNPFNNNS LINKYQSLIN QINTLEDELK TLTDSELRAT SFKLKKQYAE SKNLESLIPK
SFALTREASL RTLGLRHFDV QLIGGLVLND KKIAEMKTGE GKTLVATLPA YLNALTEKGV
HIVTVNDYLA NRDQVSMGQI YRFLGLNTGL IQDGMPNFDR RENYKADITY VTNYEVTFDF
LRDNMALNLK DVVLRPFNYC IIDEVDSILI DEAQTPLIIS NNIQTPIEKY IVAAEITDYL
ELNTHYKVDE KNKNVILTED GSKQIEQILS VQDLYDPRDP WIPYIINALK ANALYFNNVH
YIVQNNRIII VDEFTGRIMA DRRWGDGLHQ AIEAKEKLPI RQKTETVAAI TYQNFFLLYP
KLSGMTGTGK TAETEFEKIY NLSVEQIPTE RPTQRKDLPD LIYKDQFSKW NAVAQNCNQI
AKIGQPILVG TTTVEKSEML AQLLSEYKLS YQILNAKPEN VRRESEIVAQ AGKKGSITIA
TNMAGRGTDI ILGGNINFKI QKKLYDILTL VKNFKRSKKE NIFSSSLLSQ FEGSSQKFLS
VLVSLSNDQK FLKLSDLDIL KILRENDCIS IPITSYQCSI RYLIDELITY NKKHQEQENQ
IVKNLGGLYI IGTERNDSRR VDNQLRGRCG RQGDPGTSRF FLSLDDNLLR LFGGSKIQNF
MQTQIPDDSP LESEFITKSL DSAQERVEER AYQQRKNLFD YDDVLNKQRN IVYHERRNIL
ESISVQKNIF AYGEQIITEL LIELKEDKSC NIEATNLIEN LFGRNLVLNY IKTSSLSISN
LDLSELKIYL FNEFWLTYQS KITELSIYGE GIIENLERSI ILINTDRIWR EHLQKMTLLR
EAVGWRGYGQ RNPLYEYKQD AFYMFETREE LLRHLVIYDL LRSSIL
