SECA_CYAM1
ID SECA_CYAM1 Reviewed; 774 AA.
AC Q85G35;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC Cyanidioschyzon.
OX NCBI_TaxID=280699;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3377 / 10D;
RX PubMed=12755171; DOI=10.1093/dnares/10.2.67;
RA Ohta N., Matsuzaki M., Misumi O., Miyagishima S.-Y., Nozaki H., Tanaka K.,
RA Shin-i T., Kohara Y., Kuroiwa T.;
RT "Complete sequence and analysis of the plastid genome of the unicellular
RT red alga Cyanidioschyzon merolae.";
RL DNA Res. 10:67-77(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB002583; BAC76156.1; -; Genomic_DNA.
DR RefSeq; NP_848994.1; NC_004799.1.
DR AlphaFoldDB; Q85G35; -.
DR SMR; Q85G35; -.
DR STRING; 45157.CMV071CT; -.
DR PRIDE; Q85G35; -.
DR EnsemblPlants; CMV071CT; CMV071CT; CMV071C.
DR GeneID; 845020; -.
DR Gramene; CMV071CT; CMV071CT; CMV071C.
DR KEGG; cme:CymeCp062; -.
DR eggNOG; ENOG502QS7I; Eukaryota.
DR HOGENOM; CLU_005314_3_2_1; -.
DR BRENDA; 7.4.2.4; 1768.
DR Proteomes; UP000007014; 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; 2.
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..774
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000318486"
FT BINDING 66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 84..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 774 AA; 89750 MW; 5D4863528A08B2FA CRC64;
MKNKLRQIKE NREKYRKLKE EELREKTKQL KERAKQESLE ELMVEAYSNV WEGAARVLKL
EAYDVQLIGA MVLNKGQIAE MKTGEGKSLV AAFASYLNAL SGKGVHIVTV NDYLAKRDER
WIGEVLRYLG LKTAVITNES SREERKKGYE ADVTYITNSE LGFDYLRDHM AWSKEEIVQR
EFNYCIIDEV DSILIDEART PLIISGPTKG SEKPYKVAWE IGKRMKEGED YELEEKSKQV
ILKEKGIKRC EEALEVKDIF SMETPWAHYV MNAIKAKHFY IKDVNYIIKE GEVVIVDEFT
GRIMGGRRWA DGLHQAIEAK EGVKIQEESE TLASITYQNL FLLYPKLAGM TGTAKTEEEE
FEQIYGLKVV SIPTHRKMKR KDYPDVVYRT SRSKWMAVAE ECERMWTKGR PVLVGTTSIE
KSELLARLLE EKGVKYKLLN ARPSLAADEA SIIAQAGKIG SITIATNMAG RGTDIILGGN
IKEAFGEWIK ERKKQVDIEE EWRKVLEGKA DEESEKKYKQ LKEEHEKEQK RVKQLGGLYV
IGTERHESRR IDNQLRGRSG RQGDEGSSRF FISLEDDLLR IFGGGQMGEI MSRLGVEEPL
ESAFLSKSLD RAQKKVENYY YQMRKQLFEY DQVLNSQRKA IYKERTDILR SEEVGEWSKS
YIRKEWPGGL LGIKRGMRNR SEVEISYDVK KMQMESVQAG LMNELERLLL LQQIDKSWSK
HLKEMSLLRE FIAWRGYAQR DPLVEYKNES YNLFIKMIEE IRQGYAYSLF RSQA
