SECA_RHOOB
ID SECA_RHOOB Reviewed; 955 AA.
AC C1B1E2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=ROP_63900;
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=632772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4;
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AP011115; BAH54637.1; -; Genomic_DNA.
DR RefSeq; WP_015890092.1; NC_012522.1.
DR AlphaFoldDB; C1B1E2; -.
DR SMR; C1B1E2; -.
DR STRING; 632772.ROP_63900; -.
DR EnsemblBacteria; BAH54637; BAH54637; ROP_63900.
DR KEGG; rop:ROP_63900; -.
DR PATRIC; fig|632772.20.peg.6672; -.
DR HOGENOM; CLU_005314_3_0_11; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000002212; 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; Translocase; Translocation; Transport.
FT CHAIN 1..955
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000184242"
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; 105967 MW; DBBBD3EA89E71664 CRC64;
MPSLSLSKLL RVGEGRMVKR LKHIADHVSS LSPEVEDLTD EQLRAKTEEF RARYRDGETL
DELLPEAFAV AREASWRVID QRHFHVQIMG GAALHFGNIA EMKTGEGKTL TCVLPAYLNA
IAGDGVHVVT VNDYLAKRDS EWMGRVHRFL GLDTSVILSG MSPAERRAAY AADITYGTNN
EFGFDYLRDN MTHSLDDLVQ RGHNFAVVDE VDSILIDEAR TPLIISGPAD ASSKWYAEFA
RIAPLLKRDV HYEVDIRKRT IGVHEAGVEL VEDQLGIDNL YEAANSPLVS YLNNAIKAKE
LYTKDKDYIV RDGEVIIVDE FTGRVLVGRR YNEGMHQAIE AKEKVEIKAE NQTLATITLQ
NYFRLYDKLS GMTGTAETEA AELHQIYNLG VIPIPTNRPM VRVDNGDLIY KTEEAKFHAV
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 PIGVDYKELV
GDGDDETKDI TAEELRETLL KDAHDAYARR EAEIDGVAGE GSMRELERRV LLSVLDRKWR
EHLYEMDYLK EGIGLRAMAQ RDPLVEYQRE GFDMFGGMLE GLKEESVGFL FNLQVEAAAP
QAAQAPGVSV TAASAAATAS AAPAPAAPRP LPTQEAAQQA QGTAAPSALR AKGLDDGEPR
GLTYSGPAED GNAQLSRRGA AESDDSADAG TRRQRREAAR SQSKGKKAPR TKRKR
