SECA1_MYCTU
ID SECA1_MYCTU Reviewed; 949 AA.
AC P9WGP5; L0TF13; O05885; P0A5Y8; P71494;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Protein translocase subunit SecA 1 {ECO:0000255|HAMAP-Rule:MF_01382};
DE Short=tbSecA;
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA1 {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=Rv3240c;
GN ORFNames=MTCY20B11.15c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-892 IN A DIMERIC FORM WITH AND
RP WITHOUT BOUND ADP-BETA-S.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12606717; DOI=10.1073/pnas.0538077100;
RA Sharma V., Arockiasamy A., Ronning D.R., Savva C.G., Holzenburg A.,
RA Braunstein M., Jacobs W.R. Jr., Sacchettini J.C.;
RT "Crystal structure of Mycobacterium tuberculosis SecA, a preprotein
RT translocating ATPase.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2243-2248(2003).
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 (By similarity). Monomer and homodimer.
CC {ECO:0000250}.
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; AL123456; CCP46059.1; -; Genomic_DNA.
DR PIR; B70592; B70592.
DR RefSeq; WP_003901576.1; NZ_NVQJ01000003.1.
DR RefSeq; YP_177950.1; NC_000962.3.
DR PDB; 1NKT; X-ray; 2.60 A; A/B=2-892.
DR PDB; 1NL3; X-ray; 2.80 A; A/B=2-892.
DR PDBsum; 1NKT; -.
DR PDBsum; 1NL3; -.
DR AlphaFoldDB; P9WGP5; -.
DR SMR; P9WGP5; -.
DR STRING; 83332.Rv3240c; -.
DR PaxDb; P9WGP5; -.
DR DNASU; 888860; -.
DR GeneID; 45427234; -.
DR GeneID; 888860; -.
DR KEGG; mtu:Rv3240c; -.
DR TubercuList; Rv3240c; -.
DR eggNOG; COG0653; Bacteria.
DR OMA; MVHYDVQ; -.
DR PhylomeDB; P9WGP5; -.
DR BRENDA; 7.4.2.5; 3445.
DR Reactome; R-HSA-1222387; Tolerance of reactive oxygen produced by macrophages.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IDA:MTBBASE.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0015462; F:ABC-type protein transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:MTBBASE.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:MTBBASE.
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 GO; GO:0043952; P:protein transport by the Sec complex; IDA:MTBBASE.
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; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Cytoplasm; Membrane;
KW Nucleotide-binding; Protein transport; Reference proteome; Translocase;
KW Translocation; Transport.
FT CHAIN 1..949
FT /note="Protein translocase subunit SecA 1"
FT /id="PRO_0000109598"
FT REGION 869..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..938
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT HELIX 2..7
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 12..26
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 28..32
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 36..51
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 59..78
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 132..148
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 178..188
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 232..244
FT /evidence="ECO:0007829|PDB:1NKT"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:1NKT"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 264..274
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 287..300
FT /evidence="ECO:0007829|PDB:1NKT"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 334..341
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 350..356
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 358..362
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 365..373
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 379..386
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 412..428
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 433..438
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 440..452
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 465..473
FT /evidence="ECO:0007829|PDB:1NKT"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 481..485
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 500..510
FT /evidence="ECO:0007829|PDB:1NKT"
FT TURN 515..517
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 519..536
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 539..546
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 549..554
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 561..569
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 573..575
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 578..585
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 589..593
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 596..605
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 617..663
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 669..686
FT /evidence="ECO:0007829|PDB:1NKT"
FT STRAND 689..691
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 698..708
FT /evidence="ECO:0007829|PDB:1NKT"
FT TURN 715..718
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 736..758
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 762..793
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 794..796
FT /evidence="ECO:0007829|PDB:1NKT"
FT HELIX 803..832
FT /evidence="ECO:0007829|PDB:1NKT"
SQ SEQUENCE 949 AA; 106022 MW; D46C3315835E03D7 CRC64;
MLSKLLRLGE GRMVKRLKKV ADYVGTLSDD VEKLTDAELR AKTDEFKRRL ADQKNPETLD
DLLPEAFAVA REAAWRVLDQ RPFDVQVMGA AALHLGNVAE MKTGEGKTLT CVLPAYLNAL
AGNGVHIVTV NDYLAKRDSE WMGRVHRFLG LQVGVILATM TPDERRVAYN ADITYGTNNE
FGFDYLRDNM AHSLDDLVQR GHHYAIVDEV DSILIDEART PLIISGPADG ASNWYTEFAR
LAPLMEKDVH YEVDLRKRTV GVHEKGVEFV EDQLGIDNLY EAANSPLVSY LNNALKAKEL
FSRDKDYIVR DGEVLIVDEF TGRVLIGRRY NEGMHQAIEA KEHVEIKAEN QTLATITLQN
YFRLYDKLAG MTGTAQTEAA ELHEIYKLGV VSIPTNMPMI REDQSDLIYK TEEAKYIAVV
DDVAERYAKG QPVLIGTTSV ERSEYLSRQF TKRRIPHNVL NAKYHEQEAT IIAVAGRRGG
VTVATNMAGR GTDIVLGGNV DFLTDQRLRE RGLDPVETPE EYEAAWHSEL PIVKEEASKE
AKEVIEAGGL YVLGTERHES RRIDNQLRGR SGRQGDPGES RFYLSLGDEL MRRFNGAALE
TLLTRLNLPD DVPIEAKMVT RAIKSAQTQV EQQNFEVRKN VLKYDEVMNQ QRKVIYAERR
RILEGENLKD QALDMVRDVI TAYVDGATGE GYAEDWDLDA LWTALKTLYP VGITADSLTR
KDHEFERDDL TREELLEALL KDAERAYAAR EAELEEIAGE GAMRQLERNV LLNVIDRKWR
EHLYEMDYLK EGIGLRAMAQ RDPLVEYQRE GYDMFMAMLD GMKEESVGFL FNVTVEAVPA
PPVAPAAEPA ELAEFAAAAA AAAQQRSAVD GGARERAPSA LRAKGVASES PALTYSGPAE
DGSAQVQRNG GGAHKTPAGV PAGASRRERR EAARRQGRGA KPPKSVKKR
