SECA_STACT
ID SECA_STACT Reviewed; 842 AA.
AC P47994; B9DJM2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 134.
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=Sca_0401;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION OF COMPLEMENTATION
RP IN E.COLI AND B.SUBTILIS.
RX PubMed=7557338; DOI=10.1016/0378-1097(95)00267-9;
RA Klein M., Meens J., Freudl R.;
RT "Functional characterization of the Staphylococcus carnosus SecA protein in
RT Escherichia coli and Bacillus subtilis secA mutant strains.";
RL FEMS Microbiol. Lett. 131:271-277(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/aem.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
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 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: Complements temperature-sensitive (ts) secA mutants in
CC B.subtilis but does not function as well complementing ts mutants in
CC E.coli.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X79725; CAA56162.1; -; Genomic_DNA.
DR EMBL; AM295250; CAL27315.1; -; Genomic_DNA.
DR PIR; S47149; S47149.
DR RefSeq; WP_015899660.1; NC_012121.1.
DR AlphaFoldDB; P47994; -.
DR SMR; P47994; -.
DR STRING; 396513.SCA_0401; -.
DR GeneID; 60545902; -.
DR KEGG; sca:SCA_0401; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_9; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR BioCyc; SCAR396513:SCA_RS02045-MON; -.
DR Proteomes; UP000000444; 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: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 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; Translocase; Translocation;
KW Transport; Zinc.
FT CHAIN 1..842
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000109609"
FT REGION 798..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..819
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 828
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 830
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 839
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 CONFLICT 127
FT /note="G -> A (in Ref. 1; CAA56162)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="S -> R (in Ref. 1; CAA56162)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="K -> KGK (in Ref. 1; CAA56162)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 842 AA; 96056 MW; CF03D36F0037A5D8 CRC64;
MGFLTKIVDG NKREIKRLSK QADKVISLEE EMSILTDEEI RNKTKAFQER LQAEEDVSKQ
DKILEEILPE AFALVREGAK RVFNMTPYPV QIMGGIAIHN GDISEMRTGE GKTLTATMPT
YLNALAGRGV HVITVNEYLA SSQSEEMAEL YNFLGLSVGL NLNSLSTEQK REAYNADITY
STNNELGFDY LRDNMVNYSE ERVMRPLHFA IIDEVDSILI DEARTPLIIS GEAEKSTSLY
TQANVFAKML KAEDDYNYDE KTKSVQLTDQ GADKAERMFK LDNLYDLKNV DIITHINTAL
RANYTLQRDV DYMVVDGEVL IVDQFTGRTM PGRRFSEGLH QAIEAKEGVQ IQNESKTMAS
ITFQNYFRMY NKLAGMTGTA KTEEEEFRNI YNMTVTQIPT NRPVQREDRP DLIFISQKGK
FDAVVEDVVE KHKKGQPILL GTVAVETSEY ISQLLKKRGV RHDVLNAKNH EREAEIVSTA
GQKGAVTIAT NMAGRGTDIK LGEGVEELGG LAVIGTERHE SRRIDDQLRG RSGRQGDRGE
SRFYLSLQDE LMVRFGSERL QKMMGRLGMD DSTPIESKMV SRAVESAQKR VEGNNFDARK
RILEYDEVLR KQREIIYGER NNIIDSESSS ELVITMIRST LDRAISYYVN EELEEIDYAP
FINFVEDVFL HEGEVKEDEI KGKDREDIFD TVWAKIEKAY EAQKANIPDQ FNEFERMILL
RSIDGRWTDH IDTMDQLRQG IHLRSYGQQN PLRDYQNEGH QLFDTMMVNI EEDVSKYILK
SIITVDDDIE RDKAKEYQGQ HVSAEDGKEK VKPQPVVKDN HIGRNDPCPC GSGKKYKNCC
GK
