ID   SECA_RHOJR              Reviewed;         955 AA.
AC   Q0S2Y0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 116.
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=RHA1_ro06329;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(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: 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   -!- SEQUENCE CAUTION:
CC       Sequence=ABG98106.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000431; ABG98106.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011598264.1; NC_008268.1.
DR   AlphaFoldDB; Q0S2Y0; -.
DR   SMR; Q0S2Y0; -.
DR   STRING; 101510.RHA1_ro06329; -.
DR   EnsemblBacteria; ABG98106; ABG98106; RHA1_ro06329.
DR   KEGG; rha:RHA1_ro06329; -.
DR   PATRIC; fig|101510.16.peg.6380; -.
DR   eggNOG; COG0653; Bacteria.
DR   HOGENOM; CLU_005314_3_0_11; -.
DR   Proteomes; UP000008710; 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; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000185; SecA.
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; PS51196; SECA_MOTOR_DEAD; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW   Protein transport; Reference proteome; Translocase; Translocation;
KW   Transport.
FT   CHAIN           1..955
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000318416"
FT   REGION          861..955
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        921..944
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         105..109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         494
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   955 AA;  105731 MW;  46A10CBF680F77C5 CRC64;
     MPSLSLSKLL RVGEGRMVKR LKHIADHVSS LSPEVEDLTD EQLRAKTEEF RARYRDGETL
     DELLPEAFAV AREASWRVID QRHFHVQIMG GAALHFGNIA EMKTGEGKTL TCVLPAYLNA
     IAGDGVHVVT VNDYLAKRDS EWMGRVHRFL GLDTSVILSG MSPAERRAAY AADITYGTNN
     EFGFDYLRDN MTHSLDDLVQ RGHSFAVVDE VDSILIDEAR TPLIISGPAD ASSKWYAEFA
     RIAPLLKRDV HYEVDIRKRT IGVHEAGVEL VEDQLGIDNL YEAANSPLVS YLNNAIKAKE
     LYTKDKDYIV REGEVIIVDE FTGRVLVGRR YNEGMHQAIE AKEKVEIKAE NQTLATITLQ
     NYFRLYDKLS GMTGTAETEA AELHQIYNLG VIPIPTNRPM VRVDNGDLIY KTEEAKFDAV
     VDDVVERHEK GQPVLIGTTS VERSEYLSKQ FTKRGVAHNV LNAKFHEQEA QIIAEAGRSG
     AVTVATNMAG RGTDVVLGGN PDIIADIALR KQGLDPVHTP DDYEAAWDDV LDQVKAEVKA
     DADKVREAGG LYVLGTERHE SRRIDNQLRG RSGRQGDPGE SRFYLSLGDE LMRRFNGAAL
     ESIMTRLNLP DDVPIEAKMV SKAIKSAQTQ VEQQNFEIRK NVLKYDEVMN QQRTVIYNER
     RQILEGKDME GQVEKMITDV VTAYVDGATA EGYVEDWDLE QLWTALKTLY PVGVDYKELV
     GDGDGETNDI TADELRETLL TDAHDAYARR EAEIDGVAGA GSMRELERRV LLSVLDRKWR
     EHLYEMDYLK EGIGLRAMAQ RDPLVEYQRE GFDMFGGMLE GLKEESVGFL FNLQVEAAAP
     QAAQAPGVSV TAASAAATAA ASPAPAAPRP LPTQEAAQQA QGTAAPSALR AKGLDDGEPR
     GLTYSGPAED GNAQLSRRGA AESDDAADAG TRRQRREAAR SQSKGKKAPR TKRKR