SECA_STRGR
ID SECA_STRGR Reviewed; 940 AA.
AC P95759;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 03-AUG-2022, entry version 103.
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 griseus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN LEVELS, AND CHARACTERIZATION OF
RP LACK OF COMPLEMENTATION IN E.COLI.
RC STRAIN=N2-3-11;
RX PubMed=9368356; DOI=10.1111/j.1574-6968.1997.tb12700.x;
RA Poehling S., Piepersberg W., Wehmeier U.F.;
RT "Protein secretion in Streptomyces griseus N2-3-11: characterization of the
RT secA gene and its growth phase-dependent expression.";
RL FEMS Microbiol. Lett. 156:21-29(1997).
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 -!- INDUCTION: No mRNA is detectable in stationary phase cells; the protein
CC is subject to protein degradation in stationary phase.
CC -!- MISCELLANEOUS: Does not complement E.coli temperature-sensitive secA
CC mutants.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; Y10980; CAA71873.1; -; Genomic_DNA.
DR AlphaFoldDB; P95759; -.
DR SMR; P95759; -.
DR STRING; 1911.GCA_001715295_04386; -.
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..940
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000109614"
FT REGION 851..940
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 505
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 940 AA; 105178 MW; 2CEC807AA3F554A7 CRC64;
MSVFNKLMRA GEGKILRKLH RIADQVSSIE EDFVNLSDAE LRALTDEYKE RYADGESLDD
LLPEAFATVR EAAKRVLGQR HYDVQMMGGV ALHLGYVAEM KTGEGKTLVG TLPAYLNALS
GKGVHLITVN DYLAERDSEL MGRVHKFLGL SVGCIVANMT PAQRREQYGC DITYGTNNEF
GFDYLRDNMA WSKDELVQRG HNFAVVDEVD SILVDEARTP LIISGPADQP PSGTADFAKL
VTRLTKGEAG NQLKGIEETG DYEVDEKKRT VAIHEAGVAK VEDWLGIDNL YESVNTPLVG
YLNNAIKAKE LFKKDKDYVV IDGEVMIVDE HTGRILAGRR YNEGMHQAIE AKEGVDIKDE
NQTLATITLQ QNFFRLYDKL SGMTGTAMTE AAEFHQIYKL GVVPIPTNRP MVRADQSDLI
YRTEVAKFAA VVDDIAEKHE KGQPILVGTT SVEKSEYLSQ QLSKRGVQHE VLNAKQHDRE
ATIVAQAGRK GAVTVATNMA GRGTDIKLGG NPDDLAEAEL RQRGLDPVEN VEEWAAALPA
ALETAEQAVK AEFEEVKDLG GLYVLGTERH ESRRIDNQLR GRSGRQGDPG ESRFYLSLGD
DLMRLFKAQM VERVMSMANV PDDVPIENKM VTRAIASAQS QVEQQNFETR KNVLKYDEVL
NRQREVIYGE RRRVLEGEDL QEQIRHFMDD TIDDYIRQET AEGFAEEWDL DRLWGAFKQL
YPVKVTVDEL EEAAGDLAGV TAEFIAESVK NDIHEQYEER ENTLGSDIMR ELEPRWVLSV
LDRKWREHLY EMDYLQEGIG LRAMAQKDPL VEYQREGFDM FNAMMEGIKE ESVGYLFNLE
VQVEQQVEEV PVQDGAERPS LEKEGATAAP QIRAKGLEAP QRPDRLHFSA PTVDGEGGVV
EGDFANDEAT GDTRSGSADG MTRADAARRR KGGGGRRRKK
