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Database: UniProt
Entry: A0A059DDZ3_EUCGR
LinkDB: A0A059DDZ3_EUCGR
Original site: A0A059DDZ3_EUCGR 
ID   A0A059DDZ3_EUCGR        Unreviewed;       953 AA.
AC   A0A059DDZ3;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Protein translocase subunit SecA {ECO:0000256|RuleBase:RU003874};
GN   ORFNames=EUGRSUZ_A01004 {ECO:0000313|EMBL:KCW88636.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW88636.1};
RN   [1] {ECO:0000313|EMBL:KCW88636.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW88636.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + chloroplast-proteinSide 1 = ADP + phosphate +
CC         chloroplast-proteinSide 2.; EC=7.4.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034043};
CC   -!- SIMILARITY: Belongs to the SecA family. {ECO:0000256|ARBA:ARBA00007650,
CC       ECO:0000256|RuleBase:RU003874}.
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DR   EMBL; KK198753; KCW88636.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059DDZ3; -.
DR   EnsemblPlants; KCW88636; KCW88636; EUGRSUZ_A01004.
DR   Gramene; KCW88636; KCW88636; EUGRSUZ_A01004.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016464; F:chloroplast protein-transporting ATPase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0017038; P:protein import; IEA:InterPro.
DR   GO; GO:0006605; P:protein targeting; IEA:InterPro.
DR   CDD; cd17928; DEXDc_SecA; 1.
DR   CDD; cd18803; SF2_C_secA; 1.
DR   Gene3D; 1.10.3060.10; Helical scaffold and wing domains of SecA; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   Gene3D; 3.90.1440.10; SecA, preprotein cross-linking domain; 1.
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   NCBIfam; TIGR00963; secA; 1.
DR   PANTHER; PTHR30612:SF0; CHLOROPLAST PROTEIN-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR30612; SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM; 1.
DR   Pfam; PF21090; P-loop_SecA; 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; SSF81886; Helical scaffold and wing domains of SecA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF81767; Pre-protein crosslinking domain of SecA; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS01312; SECA; 1.
DR   PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003874};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003874};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|RuleBase:RU003874};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Translocation {ECO:0000256|ARBA:ARBA00023010,
KW   ECO:0000256|RuleBase:RU003874};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003874}.
FT   DOMAIN          7..672
FT                   /note="SecA family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51196"
FT   DOMAIN          93..244
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          617..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          892..953
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        899..943
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   953 AA;  107232 MW;  EE143B0A631BA3C6 CRC64;
     MASLGGLLGG IFKGGDTGES TRQQYAGTVS VINGLEAEIS ALSDSELRDR TSVLKQRAQR
     GESLDSLLPE AFAVVREASK RVLGLRPFDV QLIGGMVLHK GEIAEMRTGE GKTLVAILPA
     YLNALSGKGV HVVTVNDYLA RRDCEWVGQV PRFLGLKVGL IQQNLTSEQR RESYLCDITY
     VTNSELGFDY LRDNLATETR TPLIVSGPAE KPSDRYYKAA KVAAAFERDI HYTVDEKQKT
     VLLTEQGYED AEEILEVKDL YDPREQWALY ILNAIKAKEL FLRDVNYIIR GKEVLIVDEF
     TGRVMQGRRW SDGLHQAVEA KEGMPIQNET VTLASISYQN FFLQFPKLCG MTGTAATETA
     EFESIYKLKV TIVPTNKPMI RKDESDVVFR ATTGKWRAVV VEISRMYKTG RPVLVGTTSV
     EQSDLLSEQL KEVGIPHEVL NAKPENVERE AEIVAQSGRL GAVTIATNMA GRGTDIILGG
     NAEFMARLKL REMLMPRVVK PVEGVFVSVK KPPPKKTWKV NVDIFPCELS SRNTQLAEEV
     VQLAMNTWGQ RSLTELEAEE RLSYACEKGP AQDEVIAKLR SAFREIAKEF KVYTEEERQK
     VVQAGGLHVV GTERHESRRI DNQLRGRSGR QGDPGSSRFF LSLEDNIFRI FGGDRIQGLM
     RAFRVEDLPI ESKMLTKALD EAQRKVENYF FDIRKQLFEF DEVLNSQRDR VYAERRRALE
     SDDLQSLIIE YAELTMDDIL EANVGPDAPV ESWDLEKLIA KLQQYCYLLN DLTPDLLRSK
     GSSYEELQGY LRLRGQEAYM QKREIVEKQA PGLMTEAEKF LILSNIDRLW KEHLQALKFV
     QQAVGLRGYA QRDPLIEYKL EGYNLFLDMM AQIRRNVIYS IYQFQPVLVK KDEDRSQNGT
     TGKPTTNGRS SGKPDPVGVE SSSSAASPQD VCSIKSGSGM NNKPCEASFA YGQ
//
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