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
//