SECA2_MYCTU
ID SECA2_MYCTU Reviewed; 808 AA.
AC P9WGP3; L0T7S9; P66785; Q50612;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Protein translocase subunit SecA 2 {ECO:0000255|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA2 {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=Rv1821;
GN ORFNames=MTCY1A11.22c;
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).
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 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP44587.1; -; Genomic_DNA.
DR PIR; F70720; F70720.
DR RefSeq; NP_216337.1; NC_000962.3.
DR RefSeq; WP_003409221.1; NC_000962.3.
DR PDB; 4UAQ; X-ray; 2.80 A; A=31-808.
DR PDBsum; 4UAQ; -.
DR AlphaFoldDB; P9WGP3; -.
DR SMR; P9WGP3; -.
DR STRING; 83332.Rv1821; -.
DR PaxDb; P9WGP3; -.
DR GeneID; 885594; -.
DR KEGG; mtu:Rv1821; -.
DR PATRIC; fig|83332.111.peg.2027; -.
DR TubercuList; Rv1821; -.
DR eggNOG; COG0653; Bacteria.
DR OMA; WADHLAF; -.
DR PhylomeDB; P9WGP3; -.
DR BRENDA; 7.4.2.5; 3445.
DR Reactome; R-HSA-1222387; Tolerance of reactive oxygen produced by macrophages.
DR Reactome; R-HSA-9636383; Prevention of phagosomal-lysosomal fusion.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:MTBBASE.
DR GO; GO:0008320; F:protein transmembrane transporter activity; TAS:Reactome.
DR GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0051701; P:biological process involved in interaction with host; IMP:MTBBASE.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0052553; P:modulation by symbiont of host immune response; IMP:MTBBASE.
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; IMP:MTBBASE.
DR GO; GO:0052170; P:suppression by symbiont of host innate immune response; IMP:MTBBASE.
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; IPR026389; SecA_Actinobact_type.
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; TIGR04221; SecA2_Mycobac; 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..808
FT /note="Protein translocase subunit SecA 2"
FT /id="PRO_0000109599"
FT BINDING 124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 142..146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 535
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT HELIX 59..67
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:4UAQ"
FT TURN 93..97
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 101..114
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:4UAQ"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 145..158
FT /evidence="ECO:0007829|PDB:4UAQ"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 170..185
FT /evidence="ECO:0007829|PDB:4UAQ"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:4UAQ"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:4UAQ"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:4UAQ"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 248..253
FT /evidence="ECO:0007829|PDB:4UAQ"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 273..284
FT /evidence="ECO:0007829|PDB:4UAQ"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:4UAQ"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 305..314
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 329..341
FT /evidence="ECO:0007829|PDB:4UAQ"
FT TURN 345..348
FT /evidence="ECO:0007829|PDB:4UAQ"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 376..381
FT /evidence="ECO:0007829|PDB:4UAQ"
FT STRAND 392..399
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 400..404
FT /evidence="ECO:0007829|PDB:4UAQ"
FT STRAND 407..416
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 421..428
FT /evidence="ECO:0007829|PDB:4UAQ"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:4UAQ"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:4UAQ"
FT STRAND 449..453
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 454..470
FT /evidence="ECO:0007829|PDB:4UAQ"
FT STRAND 475..480
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 482..495
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 507..514
FT /evidence="ECO:0007829|PDB:4UAQ"
FT TURN 515..517
FT /evidence="ECO:0007829|PDB:4UAQ"
FT STRAND 523..531
FT /evidence="ECO:0007829|PDB:4UAQ"
FT TURN 539..542
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 546..551
FT /evidence="ECO:0007829|PDB:4UAQ"
FT STRAND 554..561
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 566..574
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 578..580
FT /evidence="ECO:0007829|PDB:4UAQ"
FT STRAND 583..590
FT /evidence="ECO:0007829|PDB:4UAQ"
FT TURN 594..596
FT /evidence="ECO:0007829|PDB:4UAQ"
FT STRAND 597..600
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 602..604
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 621..662
FT /evidence="ECO:0007829|PDB:4UAQ"
FT TURN 663..666
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 668..672
FT /evidence="ECO:0007829|PDB:4UAQ"
FT TURN 678..685
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 690..724
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 725..727
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 736..746
FT /evidence="ECO:0007829|PDB:4UAQ"
FT HELIX 749..760
FT /evidence="ECO:0007829|PDB:4UAQ"
FT STRAND 782..787
FT /evidence="ECO:0007829|PDB:4UAQ"
SQ SEQUENCE 808 AA; 88952 MW; 6AF6707CC3951D2F CRC64;
MNVHGCPRIA ACRCTDTHPR GRPAFAYRWF VPKTTRAQPG RLSSRFWRLL GASTEKNRSR
SLADVTASAE YDKEAADLSD EKLRKAAGLL NLDDLAESAD IPQFLAIARE AAERRTGLRP
FDVQLLGALR MLAGDVIEMA TGEGKTLAGA IAAAGYALAG RHVHVVTIND YLARRDAEWM
GPLLDAMGLT VGWITADSTP DERRTAYDRD VTYASVNEIG FDVLRDQLVT DVNDLVSPNP
DVALIDEADS VLVDEALVPL VLAGTTHRET PRLEIIRLVA ELVGDKDADE YFATDSDNRN
VHLTEHGARK VEKALGGIDL YSEEHVGTTL TEVNVALHAH VLLQRDVHYI VRDDAVHLIN
ASRGRIAQLQ RWPDGLQAAV EAKEGIETTE TGEVLDTITV QALINRYATV CGMTGTALAA
GEQLRQFYQL GVSPIPPNKP NIREDEADRV YITTAAKNDG IVEHITEVHQ RGQPVLVGTR
DVAESEELHE RLVRRGVPAV VLNAKNDAEE ARVIAEAGKY GAVTVSTQMA GRGTDIRLGG
SDEADHDRVA ELGGLHVVGT GRHHTERLDN QLRGRAGRQG DPGSSVFFSS WEDDVVAANL
DHNKLPMATD ENGRIVSPRT GSLLDHAQRV AEGRLLDVHA NTWRYNQLIA QQRAIIVERR
NTLLRTVTAR EELAELAPKR YEELSDKVSE ERLETICRQI MLYHLDRGWA DHLAYLADIR
ESIHLRALGR QNPLDEFHRM AVDAFASLAA DAIEAAQQTF ETANVLDHEP GLDLSKLARP
TSTWTYMVND NPLSDDTLSA LSLPGVFR
