SECA2_GEOTN
ID SECA2_GEOTN Reviewed; 788 AA.
AC A4ISX2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=GTNG_3081;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(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}.
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DR EMBL; CP000557; ABO68426.1; -; Genomic_DNA.
DR RefSeq; WP_011888224.1; NC_009328.1.
DR AlphaFoldDB; A4ISX2; -.
DR SMR; A4ISX2; -.
DR STRING; 420246.GTNG_3081; -.
DR EnsemblBacteria; ABO68426; ABO68426; GTNG_3081.
DR KEGG; gtn:GTNG_3081; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_2_9; -.
DR OMA; IGQIHEF; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000001578; 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; -; 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; IPR030908; SecA2_Bac_anthr.
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 TIGRFAMs; TIGR04397; SecA2_Bac_anthr; 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..788
FT /note="Protein translocase subunit SecA 2"
FT /id="PRO_0000318358"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 104..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 788 AA; 90286 MW; CDFD25E0132E3F97 CRC64;
MLSLLKRAIG YTNERQLKKY MRVVEQINRM EPQMEKLTDA ELRRKTDEFK EQLASGKSVN
DIQVEAFAVV REVAKRVLGM RHFDVQLIGG LVLAEGNIAE MATGEGKTLV ASLPSYLRAL
EGKGVHVITA NDYLAKRDRN LIGQIHEFLG LTVGLNLPLM SPQEKKQAYQ ADITYGIGTE
FGFDYLRDHM VYDASDKVQR PYHYAIIDEI DSVLIDEAKT PLIIAGKTRS STELHYIAAR
LVKRFEREVD YIYDGETKTV NLTDEGIEKV EKAFGIDNLY DAEHQVLYHY VIQALRAHVL
FQRDVDYIIR DGKVLLVDAF TGRVMEGRSL SDGLHQAIEA KEGLEITEEN KTYASITIQN
YFRMYPILSG MTGTAKTEEK EFQRIYGIDV IPIPTNRPKI RVDLPDRVYM TRHDKYVAVA
KEVKRRHESG QPVLIGTTSI LQSEEVAKYL DQEQVPYELL NAKTVEQEAE VIARAGQRGR
VTIATNIAGR GTDILLGEGV NELGGLHVLG TERHESRRID NQLKGRAGRQ GDPGSSQFFI
SLEDDMFRRF AAEETEKLKA KLKTDETGCI LNNDIHEFVD KVQRIVEGMN FSVREYNLKL
DDVMNEQRNV IYQIRDRVLE ENDRVALVVP MIRSACDRIV DAYALSEQIP EEWDVRRMTE
ELNRIVYRTP ITFDQPPADL EDVKRKVAEA VESYVALLEK KKAHTQLQTL LKSVMLTVID
DYWMRHLDQM ALLKEGIGLR HYQQEDPIRL YQKEGFEMFK AMYEVIEKEI SVHTARLLQS
LEQEEGQS
