SECA_THET2
ID SECA_THET2 Reviewed; 997 AA.
AC Q72J92;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=TT_C0887;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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; AE017221; AAS81231.1; -; Genomic_DNA.
DR RefSeq; WP_011173314.1; NC_005835.1.
DR AlphaFoldDB; Q72J92; -.
DR SMR; Q72J92; -.
DR STRING; 262724.TT_C0887; -.
DR PRIDE; Q72J92; -.
DR EnsemblBacteria; AAS81231; AAS81231; TT_C0887.
DR KEGG; tth:TT_C0887; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_0; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000000592; 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; 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..997
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000321025"
FT REGION 950..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 997 AA; 113939 MW; 9E799EC50A7FC6C9 CRC64;
MLGLLRRLFD NNEREIARYY KQVVEPVNRL EAEVEKLPDL AAAYRELKEK HEKGASLDEL
LPMAFALTRE SAKRYLGMRH FDVQLIGGAV LHEGKIAEMK TGEGKTLVAT LAVALNALTG
KGVHVVTVND YLARRDAEWM GPVYRGLGLS VGVIQHASTP AERRKAYLAD VTYVTNSELG
FDYLRDNMAI SPDQLVLRHD HPLHYAIIDE VDSILIDEAR TPLIISGPAE KATDLYYKMA
EIAKKLERGL PAEPGVRKEP TGDYTVEEKN RSVHLTLQGI AKAEKLLGIE GLFSPENMEL
AHMLIQAIRA KELYHRDRDY IVQDGQVIIV DEFTGRLMPG RRYGEGLHQA IEAKEGVRIE
RENQTLATIT YQNFFRLYEK RAGMTGTAKT EEKEFQEIYG MDVVVVPTNR PVVRKDFPDV
VYRTEKGKFY AVVEEIAEKY ERGQPVLVGT ISIEKSERLS QMLKEPRLYL PRLEMRLELF
KKASQKQQGP EWERLRKLLE RPAQLKDEDL APFEGLIPPK GNLRTAWEGL KRAVHTLAVL
RQGIPHQVLN AKHHAREAEI VAQAGRSKTV TIATNMAGRG TDIKLGGNPE YLAAALLEKE
GFDRYEWKVE LFIKKMVAGK EEEARALAQE LGIREELLER IREIREECKQ DEERVRALGG
LFIIGTERHE SRRIDNQLRG RAGRQGDPGG SRFYVSFDDD LMRLFASDRV IAMLDRMGFD
DSEPIEHPMV TRSIERAQKR VEDRNFAIRK QLLQFDDVLS RQREVIYAQR RLILLGKDEE
VKEAAIGMVE ETVASLAENF LNPEVHPEDW DLEGLKATLL DTAPQLQDFP FAELRALKAE
EAVERLVEAA LKAYEAREAE LSPPLMRAVE RFVILNVVDN AWKEHLHNLD VLRQGIFLRG
YGQKDPFQEY KIEATRLFNE MVAFIKSEVA KFLFRLKVEA EPVRPVREAP YVPVPEAKPE
PSEVFGVERK RATPPPQPGL SRAERRRLMR QEKKRKK
