SECA_THEAB
ID SECA_THEAB Reviewed; 856 AA.
AC B7ICY9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=THA_1422;
OS Thermosipho africanus (strain TCF52B).
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX NCBI_TaxID=484019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCF52B;
RX PubMed=19124572; DOI=10.1128/jb.01448-08;
RA Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT the Firmicutes and Archaea.";
RL J. Bacteriol. 191:1974-1978(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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01382}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}.
CC Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-
CC 50. {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; CP001185; ACJ75866.1; -; Genomic_DNA.
DR RefSeq; WP_012580218.1; NC_011653.1.
DR AlphaFoldDB; B7ICY9; -.
DR SMR; B7ICY9; -.
DR STRING; 484019.THA_1422; -.
DR PRIDE; B7ICY9; -.
DR EnsemblBacteria; ACJ75866; ACJ75866; THA_1422.
DR KEGG; taf:THA_1422; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_0; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000002453; 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; 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 PROSITE; PS01312; SECA; 1.
DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm; Membrane;
KW Nucleotide-binding; Protein transport; Reference proteome; Translocase;
KW Translocation; Transport.
FT CHAIN 1..856
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000145071"
FT BINDING 77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 95..99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 534
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 856 AA; 99194 MW; BAF4EE5DFFA85E39 CRC64;
MKLFDKNERV IKKYWKKVNK INKINLESKN LTELINSLKT IKENITPENI DEYIPEVFAI
VREVSKRVIG LRPFDVQLIG AMVLHEGKVA EMKTGEGKTL VATMPVVLNA LLGKGVHLVT
VNDYLAKRDA MWMGPIYLAL GLRVGVINTQ NKSYEVIWKN EELAKKALNE NLSVWPQGFN
GEFLEDEAKN KEALEAYQVE LKEISRKEAY ECDITYGTNT EFGFDYLRDN LVIDLEDRVQ
RGHFYAIVDE VDSILIDEAR TPLIISGPSK TKASDYIRFN QIAKKLVKDK HFTIDEQKKS
VILTDEGIEY IEKLLNIENL YDPEHVNKMY FLLNALKAHY LFKKDVDYII HNGEIVIVDE
FTGRLLPGRR YSGGLHQAIE AKEGVKIKEE SVTYATITYQ NYFRMYEKLS GMTGTAKTEE
EEFKQIYGME VVVIPTHKPM IRIDRDDLIY RTEDEKFEAV VKEIKKRYEK GQPVLVGTTS
IEKSERLSKM LSKEKIPHNV LNAKHHEKEA QIVALAGQKG SVTIATNMAG RGTDIKLGPG
VKELGGLLII GTERHESRRI DNQLRGRAGR QGDPGESIFF LSLEDDIIRI FGGEKLEKIM
NLVKIEKGEP IYHPMLTKLI ERVQKKVESI NFGIRKNLLQ MDTVLDTQRR AIYSYREYLL
SGNIDEHFND AIDDFIERRL EEFCEKGVCN VEEIKESLKI LNISLDKLPD TRNELKEYLK
NLLMEKFENK KKELGEDFPK IGKFIALRVI DENWRQYLEE VEHVKEAVSL RAYGQKDPIL
EFKKETFRMF DEMMAKIFEQ TIIYTLNIRK ITDEAEKESE NELKKINTQH DEFTLVNRKE
RRVAEKKGKK KLKVKR
