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Database: UniProt
Entry: A0A2P6TR47_CHLSO
LinkDB: A0A2P6TR47_CHLSO
Original site: A0A2P6TR47_CHLSO 
ID   A0A2P6TR47_CHLSO        Unreviewed;      1417 AA.
AC   A0A2P6TR47;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Protein translocase subunit SecA {ECO:0000256|RuleBase:RU003874};
GN   ORFNames=C2E21_4566 {ECO:0000313|EMBL:PRW56540.1};
OS   Chlorella sorokiniana (Freshwater green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX   NCBI_TaxID=3076 {ECO:0000313|EMBL:PRW56540.1, ECO:0000313|Proteomes:UP000239899};
RN   [1] {ECO:0000313|EMBL:PRW56540.1, ECO:0000313|Proteomes:UP000239899}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX 1602 {ECO:0000313|Proteomes:UP000239899};
RX   PubMed=29178410; DOI=10.1111/tpj.13789;
RA   Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA   Barney B.M.;
RT   "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT   conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL   Plant J. 93:566-586(2018).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PRW56540.1}.
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DR   EMBL; LHPG02000008; PRW56540.1; -; Genomic_DNA.
DR   STRING; 3076.A0A2P6TR47; -.
DR   OrthoDB; 33963at2759; -.
DR   Proteomes; UP000239899; Unassembled WGS sequence.
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; 2.
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; 2.
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; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000239899};
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          71..779
FT                   /note="SecA family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51196"
FT   DOMAIN          157..315
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          39..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1002..1027
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1182..1211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1182..1209
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1417 AA;  156169 MW;  B747CD12F2196E4F CRC64;
     MATAGLCCTA ARATEALAAP VAARQHAALR PVPFTAVHQR GAAGRRQGSG GAAAPSASRR
     RGAARVHALL GGLGSMFKND PSERTRKQYQ SRVDAINALE PDMQKLSDAQ LRELTQALKQ
     RAAAGEPLDS LLVESFALVR EASKRVLGLR PFDVQLIGGM ILHEGQIAEM RTGEGKTLVA
     VLPSFLNALS GQGVHVVTVN DYLARRDSEW VGQVHKFLGL EVGLVQQGLN EKQRRAAYNA
     DVTYVTNSEL GFDYLRDNLA QDKEELVLRP FNFCVIDEVD SILIDEARTP LIISGTADKP
     SDKYYKAAKL AGALAKATHY TVDEKQRNVL LTEEGYEAAE DVLQVSDLYD PREQWASYIL
     NAIKAKELFI RDVSYIVRAN EAKELFIRDV SYIVRANEII IVDEFTGRTM PGRRWSDGLH
     QAIEAKEGLE IQNESVTLAS ISYQNFFRAY PKLAGMTGTA ATESAEFSQI YNLPVTVVPP
     NRTVSRTDNP DVVFRNESGK WKAVVQEIRR MHKTGRPVLV GTTSVEKSEI LAGMLEQEGI
     PYQLLNAKPE NVERESEIVA QSGRRGAVTI ATNMAGRGTD ILLGGNPEFM ARLKLRELLM
     PEVVSQVDME GGDKKSVRVR KIKSWAVSPA LFPCDLSAEA KALCQDAVKA AVSGWGERQL
     EELEAEERLA FACEKAPTSD PVIEKIRAAF LKVEAEYKQV TDVEKVEVQK LGGLHVVGTE
     RHESRRIDNQ LRGRSGRQGD QGSTRYFLSL EDNLFRIFGG DRIKGLMSAF RIEDLPIESQ
     MLTNALDEAQ RKVESYFYDI RKQLFDYDQV LNTQRDKVYA ERRRALEASD LTPLMVEYAE
     RTIDDILEAN IPPTTPPEEW PLEPLVAKLR QYCYLLEDLT PQALAAEAGG DYERMRDYLR
     KRGVEAYYRK REEMEGAEAG LSSKAERFFV LVQTDNLWKE HLQAIKFLQQ AVSLRGYAQR
     DPLVEYKLEG YNLFVEMMAQ IRRNVIYNVY MFKPAEAEAK QRAFEEEQRQ KAAAAQNGGS
     RGKGKKAAPA AAPCQGCAVH GTNAPLACPI VVLTVTQPIW TAHKTQMSQE RDAPKAASAR
     VVRHPAAEPS PAWAAIPNED NLPNDVHALA AALALRLGVG VLDCGWFRSV SNPGRFLCLH
     LVALNRSTGA YTLAQLESRE GLLTALHNAL GRPVWNVLPA AEGVEEEEEE EEEEEEEEEE
     EEEEEEEAGE PGAPLLRKAR HFTAQWAVVV LLLAVLALRA APTVPITSLA TALVQPLSAA
     MPAMFQRNGA GGADVTADWP PALRWLDAQP SQDDVIALLS RNDTKERLSM GNTVLHAARA
     GKEELARNCS SREIAIRKEL AAELTAIAAG VEAGQPLLPD LLAAPVRRGN STLEALSASC
     AAAKAGKDEE IKRITRLVHK LARQLELLGP GATAAAE
//
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