SECA_HYDS0
ID SECA_HYDS0 Reviewed; 944 AA.
AC B4U965;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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};
GN OrderedLocusNames=HY04AAS1_0990;
OS Hydrogenobaculum sp. (strain Y04AAS1).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobaculum;
OC unclassified Hydrogenobaculum.
OX NCBI_TaxID=380749;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y04AAS1;
RX PubMed=19136599; DOI=10.1128/jb.01645-08;
RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(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; CP001130; ACG57676.1; -; Genomic_DNA.
DR RefSeq; WP_012514032.1; NC_011126.1.
DR AlphaFoldDB; B4U965; -.
DR SMR; B4U965; -.
DR STRING; 380749.HY04AAS1_0990; -.
DR PRIDE; B4U965; -.
DR EnsemblBacteria; ACG57676; ACG57676; HY04AAS1_0990.
DR KEGG; hya:HY04AAS1_0990; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_0; -.
DR OMA; MVHYDVQ; -.
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 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 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 inner membrane; Cell membrane; Cytoplasm; Membrane;
KW Nucleotide-binding; Protein transport; Translocase; Translocation;
KW Transport.
FT CHAIN 1..944
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000145024"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 114..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 554
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 944 AA; 108806 MW; 8D25E01A236D26C4 CRC64;
MIGYVLKKIL GTKNDREIKK IRKWVEKINA LEESLDKLSN KDIVLKAQDL YFRVNQNEHI
KQAIIEGEMV EELIEAFALV REASKRTMGL RQFDVQLIGG IVLYQGKIAE MKTGEGKTLV
AAAPAFFTAL TDTGVHVVTV NDYLAKRDAT WIGPIYRFLG LDVGVINSDN MSYIIDWQDP
EKAMEAIEKD IRVWPKGMVG DAIDYSKIDV HAKTSYFTKA ISVERAKAYE AHITYGTNNE
FGFDYLRDNL AVSKDQIVQV KGHGYAIVDE IDSILIDEAR TPLIIAGPSN LDNKVVLQAN
EFVQTLEIEK DFIVDEKNRT AMLTEEGIEK AEKYFNIQNL YDIRHIDLVH AINKALLAHN
LYKKDVHYMV KDGEILIVDE FTGRALPGRR WSEGLHQAIE AKEGVEIQEE NQTLATTAFQ
NYFKLYKKLA GMTGTAETEA LEFKEIYSLD VVVIPTNKPN IRKDLPDAIF KTKKEKWEYI
AKVIEENHAK GRPILVGTVS IEDSETLSKL LEQRGIKHNV LNAKQHEKEA WIIAQAGRKG
AVTIATNMAG RGTDILLGGN PEFLAREILK QKGIDEDKAT EEEWKQAYEE ATKITQKEKE
EVIKAGGLLV IGTERHESRR VDNQLRGRAG RQGDPGESRF ILSLEDDLLR IFGGDRVKKL
MEFMKIPEGE PIESSIVSKS LEGAQERVEL QNFQSRKRLL EYDEVINIQR SVVYDIRRSI
LFQDDIKEEI KDFIKDVIHT QVFTLLTEDE PELWELEPLK TFFKEWIDLD LPEKFEAKDR
EELEEEIFKL VMEKYAQKEQ EIGEKTMREI EKVFTLNIID NLWREQLHTI DKLREGIYLR
SYAQRDPLVE FKKEAFRLFE ELMLNFKISA IQSIMNAQIS KEELEQQEQN MFNLEIDTLN
KSMAISEALE NIAKEFQEKR PRFRTLKDRL EERKKKLEKK GESA
