SECA_THET8
ID SECA_THET8 Reviewed; 997 AA.
AC Q5SIW3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=TTHA1251;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH SECY.
RX PubMed=18923527; DOI=10.1038/nature07421;
RA Tsukazaki T., Mori H., Fukai S., Ishitani R., Mori T., Dohmae N.,
RA Perederina A., Sugita Y., Vassylyev D.G., Ito K., Nureki O.;
RT "Conformational transition of Sec machinery inferred from bacterial SecYE
RT structures.";
RL Nature 455:988-991(2008).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND SUBUNIT.
RX PubMed=17059823; DOI=10.1016/j.jmb.2006.09.061;
RA Vassylyev D.G., Mori H., Vassylyeva M.N., Tsukazaki T., Kimura Y.,
RA Tahirov T.H., Ito K.;
RT "Crystal structure of the translocation ATPase SecA from Thermus
RT thermophilus reveals a parallel, head-to-head dimer.";
RL J. Mol. Biol. 364:248-258(2006).
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: Part of the essential Sec protein translocation apparatus
CC which comprises SecA, SecYEG and auxiliary proteins SecDF. Other
CC proteins may also be involved. Monomer and homodimer.
CC {ECO:0000269|PubMed:17059823}.
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; AP008226; BAD71074.1; -; Genomic_DNA.
DR RefSeq; WP_011228548.1; NC_006461.1.
DR RefSeq; YP_144517.1; NC_006461.1.
DR PDB; 2IPC; X-ray; 2.80 A; A/B/C/D=1-997.
DR PDBsum; 2IPC; -.
DR AlphaFoldDB; Q5SIW3; -.
DR SMR; Q5SIW3; -.
DR DIP; DIP-59815N; -.
DR IntAct; Q5SIW3; 1.
DR STRING; 300852.55772633; -.
DR EnsemblBacteria; BAD71074; BAD71074; BAD71074.
DR GeneID; 3169354; -.
DR KEGG; ttj:TTHA1251; -.
DR PATRIC; fig|300852.9.peg.1230; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_0; -.
DR OMA; MVHYDVQ; -.
DR PhylomeDB; Q5SIW3; -.
DR EvolutionaryTrace; Q5SIW3; -.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm;
KW Membrane; Nucleotide-binding; Protein transport; Reference proteome;
KW Translocase; Translocation; Transport.
FT CHAIN 1..997
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000321026"
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"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 40..52
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 57..75
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 103..117
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 130..145
FT /evidence="ECO:0007829|PDB:2IPC"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 160..167
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 176..186
FT /evidence="ECO:0007829|PDB:2IPC"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 277..287
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:2IPC"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 298..312
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:2IPC"
FT TURN 332..335
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 347..354
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 371..375
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 378..387
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 392..399
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 415..424
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 425..442
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 453..464
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 466..469
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 470..484
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 490..498
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 507..510
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 512..516
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 521..542
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 554..562
FT /evidence="ECO:0007829|PDB:2IPC"
FT TURN 563..565
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 570..573
FT /evidence="ECO:0007829|PDB:2IPC"
FT TURN 577..580
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 589..595
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 606..618
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 621..630
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 635..655
FT /evidence="ECO:0007829|PDB:2IPC"
FT TURN 656..658
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 663..667
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 672..680
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 690..699
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 700..704
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 710..716
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 721..723
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 728..774
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 778..801
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 807..809
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 812..821
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 830..836
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 840..860
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 863..896
FT /evidence="ECO:0007829|PDB:2IPC"
FT STRAND 901..904
FT /evidence="ECO:0007829|PDB:2IPC"
FT HELIX 906..934
FT /evidence="ECO:0007829|PDB:2IPC"
SQ SEQUENCE 997 AA; 113953 MW; 9A22888B52698CCA 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 PVIRKDFPDV
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
