SECA_STRLI
ID SECA_STRLI Reviewed; 947 AA.
AC P0A4G7; P55021; P95725; Q54396;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 76.
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};
OS Streptomyces lividans.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1916;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION OF COMPLEMENTATION
RP OF E.COLI MUTANTS.
RC STRAIN=66 / 1326;
RX PubMed=8765222; DOI=10.1016/0167-4838(96)00075-1;
RA Gilbert M., Ostiguy S., Kluepfel D., Morosoli R.;
RT "Cloning of a secA homolog from Streptomyces lividans 1326 and
RT overexpression in both S. lividans and Escherichia coli.";
RL Biochim. Biophys. Acta 1296:9-12(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=66 / 1326;
RX PubMed=8918233; DOI=10.1016/0378-1119(96)00220-x;
RA Blanco J., Coque J., Martin J.;
RT "Characterization of the secA gene of Streptomyces lividans encoding a
RT protein translocase which complements an Escherichia coli mutant defective
RT in the ATPase activity of SecA.";
RL Gene 176:61-65(1996).
RN [3]
RP SEQUENCE REVISION TO 712-723.
RC STRAIN=66 / 1326;
RA Blanco J.;
RL Submitted (JUL-1997) 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 -!- MISCELLANEOUS: Restores azide sensitivity to E.coli azide-insensitive
CC mutants, but is not able to complement temperature-sensitive mutants.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; U21192; AAC44331.1; -; Genomic_DNA.
DR EMBL; Z50195; CAA90577.1; -; Genomic_DNA.
DR PIR; S71922; S71922.
DR AlphaFoldDB; P0A4G7; -.
DR SMR; P0A4G7; -.
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; 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 ATP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW Protein transport; Translocase; Translocation; Transport.
FT CHAIN 1..947
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000109616"
FT REGION 864..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 103..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 514
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT CONFLICT 494
FT /note="A -> R (in Ref. 2; CAA90577)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 947 AA; 106456 MW; ECE618B7890AEC51 CRC64;
MSVLSKLMRA GEGKILRKLH RIADQVNSIE EDFADLSDAE LRALTDEYKQ RYADGESLDD
LLPEAFATVR EAAKRVLGQR HYDVQIMGGA ALHMGYVAEM KTGEGKTLVG TLPAYLNALS
GEGVHIVTVN DYLAERDSEL MGRVHKFLGL NVGCILANQT PAQRREMYAC DITYGTNNEF
GFDYLRDNMA WSKDELVQRG HNFAIVDEVD SILVDEARTP LIISGPADQA TKWYGDFAKL
VTRLKKGEAG NTLKGIEETG DYEVDEKKRT VAIHESGVAK VEDWLGIDNL YESVNTPLVG
YLNNAIKAKE LFKKDKDYVV LDGEVMIVDE HTGRILAGRR YNEGMHQAIE AKEGVDIKDE
NQTLATITLQ NFFRLYKRHD HDGKEQPGLS GMTGTAMTEA AEFHQIYKLG VVPIPTNRPM
VRKDQSDLIY RTEVAKFEAV VDDIEEKHRK GQPILVGTTS VEKSEYLSQQ LSKRGVQHEV
LNAKQHDREA TIVAQAGRKG SVTVATNMAG RGTDIKLGGN PEDLAEAELR QRGLDPEEHI
EEWAAALPAA LERAEQAVKA EFEEVKELGG LYVLGTERHE SRRIDNQLRG RSGRQGDPGE
SRFYLSLGDD LMRLFKAQMV ERVMSMANVP DDVPIENKMV TRAIASAQSQ VETQNFETRK
NVLKYDEVLN RQREVIYGER RRVLEGEDLQ EQIQHFTNDT IDAYVQAETA EGFPEDWDLD
RLWGAFKQLY PVKVTVEELE EAAGDRAGLT ADYIAESIKD DVREQYEARE KQLGSEIMRE
LERRVVLSVL DRKWREHLYE MDYLQEGIGL RAMAQKDPLV EYQREGFDMF QAMMDGIKEE
SVGYLFNLEV QVEQQVEEVP VEDAAPSLDK GAQDAVPAQA GARPEIRAKG LDAPQRRDLH
FSAPTVDGEG GVVEGEFTDG EPAQAQSDGL TRAERRKQAK GGRRRKK
