SECA_DEIGD
ID SECA_DEIGD Reviewed; 869 AA.
AC Q1IZH7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=Dgeo_1058;
OS Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=319795;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11300 / AG-3a;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000359; ABF45357.1; -; Genomic_DNA.
DR RefSeq; WP_011530194.1; NC_008025.1.
DR AlphaFoldDB; Q1IZH7; -.
DR SMR; Q1IZH7; -.
DR STRING; 319795.Dgeo_1058; -.
DR PRIDE; Q1IZH7; -.
DR EnsemblBacteria; ABF45357; ABF45357; Dgeo_1058.
DR KEGG; dge:Dgeo_1058; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_2_0; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000002431; 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; IPR001650; Helicase_C.
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_0000320791"
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; 97812 MW; 62BB3D62FC1E732B CRC64;
MFRVLNKVFD TNQRDVQRIV KTVVQPVNAL EEETMKIENL AEAFMRLRQR VQEGGESLDD
VLVPAFALIR EAGRRAIGKR HYDVQLIGGT ALHQGRIAEM RTGEGKTLVA TLALALNALE
GKGAHLVTVN DYLARVGAEE MGLLYRTLGL SVGLITRDMQ PHQRQAAYAC DITYVTNSEL
GFDYLRDNMA QSREQLVLRA DNPLHYAIVD EVDSILIDEA RTPLIISGAA EKATDLYYVY
AKLVKRLQRG EPAEPGKRTE PTGDYTIDEK GKQVHLTEQG IAKIERLLSL GDLYSPENMD
KAHMITQAIR ARELYHREKD YIVNAEGEVV IIDEFTGRSM PGRRYGEGLH QAIEAKEGVK
IENENQTLAT ITYQNFFRLY DKFAGMTGTA KTEEKEFLDI YGSDVLVIPT NKPVIRQDAD
DLVYRTRMGK YQAVVEEVKQ MHATGRPILI GTASIDTSEQ LSALLKQAGI RHSVLNAKYE
AQEASIIAQA GRSGTVTIAT NMAGRGTDIM LGGNAEFILG EAIEQNFGIS RFTPEAEAFI
KAIGREDPEA VTLGLRIPGM TEQFIRQAQQ LQKDIIADRE RVRELGGLHI IGTERHESRR
IDNQLRGRAG RQGDPGSSRF YVSFEDDLMR LFASDRVVAM MDRLGMDDTQ PIEAKMVTGA
IERAQARVED RNFGIRKQLL EFDNVMSKQR DIIYAQRREV LLGTDEDVEE STEGMIADFT
EMQLAFYAPI DQPAESWDLE TLRTNMLEAV PQLEHYDFEA LRHMAPEAAH AHLLEAVADA
FDARKAELGP TMLNSLARYV LLQVVDQHWK EHLHGMDVLR QGIGLRGYGQ RDPFTEYKFE
ATNMFNDMID NLKADVTKFI FRMQFGQAS
