SECA1_STAA8
ID SECA1_STAA8 Reviewed; 843 AA.
AC O06446; Q2G054;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Protein translocase subunit SecA 1 {ECO:0000255|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA1 {ECO:0000255|HAMAP-Rule:MF_01382};
GN OrderedLocusNames=SAOUHSC_00769;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Segarra R.A., Iandolo J.J.;
RT "Molecular characterization of the Staphylococcus aureus SecA homolog.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ISP479C;
RX PubMed=18621893; DOI=10.1128/jb.00300-08;
RA Siboo I.R., Chaffin D.O., Rubens C.E., Sullam P.M.;
RT "Characterization of the accessory Sec system of Staphylococcus aureus.";
RL J. Bacteriol. 190:6188-6196(2008).
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01382};
CC Note=May bind 1 zinc ion per subunit. {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 ECO:0000269|PubMed:18621893}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01382, ECO:0000269|PubMed:18621893};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382,
CC ECO:0000269|PubMed:18621893}. Cytoplasm {ECO:0000255|HAMAP-
CC Rule:MF_01382, ECO:0000269|PubMed:18621893}. Note=Distribution is 50-
CC 50. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- INDUCTION: Expressed in log phase cells (at protein level).
CC {ECO:0000269|PubMed:18621893}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; U97062; AAB54024.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD29899.1; -; Genomic_DNA.
DR RefSeq; WP_000506531.1; NZ_LS483365.1.
DR RefSeq; YP_499326.1; NC_007795.1.
DR AlphaFoldDB; O06446; -.
DR SMR; O06446; -.
DR STRING; 1280.SAXN108_0820; -.
DR BindingDB; O06446; -.
DR ChEMBL; CHEMBL3832949; -.
DR EnsemblBacteria; ABD29899; ABD29899; SAOUHSC_00769.
DR GeneID; 3919060; -.
DR KEGG; sao:SAOUHSC_00769; -.
DR PATRIC; fig|93061.5.peg.693; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_9; -.
DR OMA; MVHYDVQ; -.
DR PRO; PR:O06446; -.
DR Proteomes; UP000008816; 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:0015462; F:ABC-type protein transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 GO; GO:0043952; P:protein transport by the Sec complex; IBA:GO_Central.
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; IPR004027; SEC_C_motif.
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; PF02810; SEC-C; 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; Metal-binding;
KW Nucleotide-binding; Protein transport; Reference proteome; Translocase;
KW Translocation; Transport; Zinc.
FT CHAIN 1..843
FT /note="Protein translocase subunit SecA 1"
FT /id="PRO_0000109608"
FT REGION 799..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 109..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 498
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 829
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 831
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 840
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 841
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT CONFLICT 254
FT /note="E -> D (in Ref. 1; AAB54024)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 843 AA; 95960 MW; DE26F80829A19102 CRC64;
MGFLSKILDG NNKEIKQLGK LADKVIALEE KTAILTDEEI RNKTKQFQTE LADIDNVKKQ
NDYLDKILPE AYALVREGSK RVFNMTPYKV QIMGGIAIHK GDIAEMRTGE GKTLTATMPT
YLNALAGRGV HVITVNEYLS SVQSEEMAEL YNFLGLTVGL NLNSKTTEEK REAYAQDITY
STNNELGFDY LRDNMVNYSE DRVMRPLHFA IIDEVDSILI DEARTPLIIS GEAEKSTSLY
TQANVFAKML KQDEDYKYDE KTKAVHLTEQ GADKAERMFK VENLYDVQNV DVISHINTAL
RAHVTLQRDV DYMVVDGEVL IVDQFTGRTM PGRRFSEGLH QAIEAKEGVQ IQNESKTMAS
ITFQNYFRMY NKLAGMTGTA KTEEEEFRNI YNMTVTQIPT NKPVQRNDKS DLIYISQKGK
FDAVVEDVVE KHKAGQPVLL GTVAVETSEY ISNLLKKRGI RHDVLNAKNH EREAEIVAGA
GQKGAVTIAT NMAGRGTDIK LGEGVEELGG LAVIGTERHE SRRIDDQLRG RSGRQGDKGD
SRFYLSLQDE LMIRFGSERL QKMMSRLGLD DSTPIESKMV SRAVESAQKR VEGNNFDARK
RILEYDEVLR KQREIIYNER NSIIDEEDSS QVVDAMLRST LQRSINYYIN TADDEPEYQP
FIDYINDIFL QEGDITEDDI KGKDAEDIFE VVWAKIEAAY QSQKDILEEQ MNEFERMILL
RSIDSHWTDH IDTMDQLRQG IHLRSYAQQN PLRDYQNEGH ELFDIMMQNI EEDTCKFILK
SVVQVEDNIE REKTTEFGEA KHVSAEDGKE KVKPKPIVKG DQVGRNDDCP CGSGKKFKNC
HGK
