SECA_DEIDV
ID SECA_DEIDV Reviewed; 869 AA.
AC C1CWX4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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}; OrderedLocusNames=Deide_17210;
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts with
CC the SecYEG preprotein conducting channel. Has a central role in
CC coupling the hydrolysis of ATP to the transfer of proteins into and
CC across the cell membrane, serving as an ATP-driven molecular motor
CC driving the stepwise translocation of polypeptide chains across the
CC membrane. {ECO:0000255|HAMAP-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 -!- SUBUNIT: Monomer and homodimer. Part of the essential Sec protein
CC translocation apparatus which comprises SecA, SecYEG and auxiliary
CC proteins SecDF. Other proteins may also be involved.
CC {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01382};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01382};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}. Cytoplasm
CC {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-50.
CC {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; CP001114; ACO46691.1; -; Genomic_DNA.
DR RefSeq; WP_012693813.1; NC_012526.1.
DR AlphaFoldDB; C1CWX4; -.
DR SMR; C1CWX4; -.
DR STRING; 546414.Deide_17210; -.
DR PaxDb; C1CWX4; -.
DR EnsemblBacteria; ACO46691; ACO46691; Deide_17210.
DR KEGG; ddr:Deide_17210; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_2_0; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000002208; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma 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; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW Protein transport; Reference proteome; Translocase; Translocation;
KW Transport.
FT CHAIN 1..869
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000215105"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 103..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 869 AA; 97107 MW; B70F1B28C3D2D69A CRC64;
MFRVLNKVFD NNQRDVQRII KTVVDPVNAL EQETMQIEDL AAAFLDLRRR VQEGGESLDD
VLVPAFALIR EAGRRSIGKR HYDVQLIGGA ALHQGRIAEM RTGEGKTLVA TLALSLNALE
GRGCHLVTVN DYLARVGMEE MGLLYRTLGL TVGLASREMQ PHEKQAAYAC DITYVTNSEL
GFDYLRDNMA QSREALAMRA EHPLNYAIVD EVDSILIDEA RTPLIISGAA EKATDLYYVY
AKLIRRLQKG EPAEPGVRAE PTGDYTIDEK GKQVHITEAG ISKIERLLSI PDLYSPENMD
KAHMITQAIR AKELYHREKD YIINADGEVI IIDEFTGRSM PGRRYGEGLH QAIEAKENVK
IENENQTLAT ITYQNFFRLY NKFAGMTGTA KTEEKEFLDI YGSDVLVIPT NRTILRKDSE
DLVYRTKMGK YAAVVQEVAE MHATGRPVLI GTASIVTSEQ LSDLLTQAGI RHSVLNAKFE
AQEASIVAQA GRSGTVTIAT NMAGRGTDIM LGGNAEFILG ESIEQHLGIS RFAPEAENFI
KAISRQDPAA EMLGMQIPGM TPEFIQQAQQ LQADTVADRA RVQELGGLHI IGTERHESRR
IDNQLRGRAG RQGDPGSSRF YVSFEDDLMR LFANDRVVAM MDRLGMDDSQ PIEAKMVTGA
IEKAQARVED RNFSTRKQLL EFDNVMSKQR DTIYAQRREV LLGPDEDVEE STEGMIADFV
DMQLAIHAPA DQSPDAWDIE GLQAAIVDAV PQLEGFDFES LRHGSPAQAQ DRLLSAVADA
FDSRREELGS TMLNSLARYV LLQVVDQHWK EHLHGMDVLR QGIGLRGYGQ RDPFTEYKFE
ATNMFNEMID NLKSDVTKFI FRMQFGQTG
