SECA_NEOYE
ID SECA_NEOYE Reviewed; 884 AA.
AC Q1XDA6;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, 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 Neopyropia yezoensis (Susabi-nori) (Pyropia yezoensis).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia.
OX NCBI_TaxID=2788;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U-51;
RA Kunimoto M., Morishima K., Yoshikawa M., Fukuda S., Kobayashi T.,
RA Kobayashi M., Okazaki T., Ohara I., Nakayama I.;
RT "Whole genome sequence of Porphyra yezoensis chloroplast.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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; AP006715; BAE92505.1; -; Genomic_DNA.
DR RefSeq; YP_537062.1; NC_007932.1.
DR AlphaFoldDB; Q1XDA6; -.
DR SMR; Q1XDA6; -.
DR GeneID; 3978773; -.
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..884
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000277298"
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 884 AA; 101426 MW; EEEA05EE0F831FED CRC64;
MFNFLFNSSN QRKINSYAPI VKKINALEIE MQDLPDKVLR AKSVQFKSRL QNGENLDDIL
VEAFAVVREA GLRVLGLRVF DVQMMGAIIL HQGKIAEMKT GEGKTLVATL AGYLNALSGE
GVHVVTVNDY LAKRDSEWVG QIHKFLGLSV GLIQQALPKV ERKLAYQCDV TYVTNSELGF
DYLKDNMVLS MSEIVQNKFA FCIIDEVDSI LIDEARTPLI ISGPSEAPIE KYSRTKLLAN
ILSKDVHYEV DEKARNIILT EQGTLFCEEY LSINNLYDLE NPWVQYILNA IKARELFTKD
VHYIIRDKEV VIVDEFTGRI MSGRRWSDGL HQAIEAKEDV VIQQENQTYA SITYQNFFLL
YPKLSGMTGT AKTEESELDK IYNLEVICVP THKPLRRKEF PDLVYSNEYR KWEAIADECY
DMYRVGRPTL VGTTSVEKSE LLSKLLNQYK IPHSLLNAKP ENVEKESDII AQAGRQSSVT
IATNMAGRGT DIILGGNPSY IAKSILVDLL IGKSSVKNNY KLQQLSPNTK ISLNNILNAL
ETDLHSVDFS MLEMEKKISI ACEQVLTDDK LEIQLRKAYQ MIFEEFETIF SKEREYVSQA
GGLHVIGTER HESRRIDNQL RGRAGRQGDP GSSRFFLSVD DNLLRIFGGN KIADLMQALN
VDNDTPMEST LLSKSLEAAQ KKVEAYFYDT RKQVFEYDQV LNSQRQAIYA ERRRILESSY
PRDCVLQYAE STIDDIITFW LTSKENPEKF VNLNIKIKYL LNAADTFSIS KDLYKDSEEL
KKWIIEQVRI NYDLREAYLE QIKPGLIRQL EKYYLLQQID NAWKDHLQKM GALRDSIGWR
SYGQQDPLVE YKNEAFNLFI EMITHVKHTV VYAILRSRLM MKND