SECA2_THEFY
ID SECA2_THEFY Reviewed; 766 AA.
AC Q47RW8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein translocase subunit SecA 2 {ECO:0000255|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA2 {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=Tfu_0761;
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=269800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX;
RX PubMed=17209016; DOI=10.1128/jb.01899-06;
RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA Kyrpides N.;
RT "Genome sequence and analysis of the soil cellulolytic actinomycete
RT Thermobifida fusca YX.";
RL J. Bacteriol. 189:2477-2486(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAZ54799.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000088; AAZ54799.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_038043394.1; NC_007333.1.
DR AlphaFoldDB; Q47RW8; -.
DR SMR; Q47RW8; -.
DR STRING; 269800.Tfu_0761; -.
DR PRIDE; Q47RW8; -.
DR EnsemblBacteria; AAZ54799; AAZ54799; Tfu_0761.
DR KEGG; tfu:Tfu_0761; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_2_11; -.
DR OrthoDB; 212453at2; -.
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 Gene3D; 3.40.50.300; -; 3.
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; IPR026389; SecA_Actinobact_type.
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; 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; TIGR04221; SecA2_Mycobac; 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; Translocase; Translocation; Transport.
FT CHAIN 1..766
FT /note="Protein translocase subunit SecA 2"
FT /id="PRO_0000318479"
FT BINDING 84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 102..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 490
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 766 AA; 84833 MW; EBC8E197A7F90821 CRC64;
MAEGVRRLLG KPGSVSLQPY IKLLKTIEER EEALRKLSDA ELTEVATELG NAELPYDRDD
LAELCALGRE AARRTLGERP FDTQLIGMMA LLDGHVAEMA TGEGKTLTGA LAAVGFALRG
QRVHVLSVND YLARRDAEWM RPLYTLLGVE VGWISQESTT EERRAAYAAD ITYASVSELG
FDVLRDRLAT DVSELVVPEP NVAIIDEADS VLVDEARVPL VLAGAAEPAE SDAAMAELVR
RLRPGIDYKV DDDGRNVHLT DTGINVVEKA LGGVDLFSAE DTTLLSRVNL ALHAHALLHR
DVHYVVRDGK VRLINESRGR IALLQRWPDG LQAAVEAKEH LTPSETGEVL DSITVQSLVL
RYPIRCGMTG TAMAVAEQLR EFYELEVAVI APNKPNIRID EEDRLYATAE EKEEAVVEKV
KEVHATGRPI LIGTQDVAES ERLAKRLRRA GLECVVLNAK NDAEEAAVIA EAGTYGRITV
STQMAGRGTD IRLGGSDMRD RDRVVKTGGL YVIGYGRYPS SRLDDQLRGR AGRQGDPGGS
VFYVSVEDDL ITTNLPEAKG YRVSSADGEI TDPAWKEMVN HAQRIAEGQL LELHRNTWRY
NQIIDVQRSV VLEQRRAVLH EDLGSRQLAV DCPETYQRLV EEVGEEEVAR AARLVTLYHL
DRGWADHNAF LADLREGIHL RFLGRRDPLD EFNRDAVPAF KGFLDEARAR AAEMFEKLEV
VDGRLDVAAA GVKRPSTTWT YMVQDQPFST DLENIVGRVK NLMGRD
