SECA1_LISMO
ID SECA1_LISMO Reviewed; 837 AA.
AC P47847;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, 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}; OrderedLocusNames=lmo2510;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Owens M.U., Berkaw M.N., Schmidt M.G.;
RT "Isolation and characterization of the secA gene from Listeria
RT monocytogenes.";
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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 -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; L32090; AAA50286.1; -; Genomic_DNA.
DR EMBL; AL591983; CAD00588.1; -; Genomic_DNA.
DR PIR; AF1388; AF1388.
DR RefSeq; NP_466033.1; NC_003210.1.
DR RefSeq; WP_003722642.1; NC_003210.1.
DR AlphaFoldDB; P47847; -.
DR SMR; P47847; -.
DR STRING; 169963.lmo2510; -.
DR PaxDb; P47847; -.
DR EnsemblBacteria; CAD00588; CAD00588; CAD00588.
DR GeneID; 985470; -.
DR KEGG; lmo:lmo2510; -.
DR PATRIC; fig|169963.11.peg.2570; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_9; -.
DR OMA; MVHYDVQ; -.
DR PhylomeDB; P47847; -.
DR BioCyc; LMON169963:LMO2510-MON; -.
DR Proteomes; UP000000817; 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; -; 3.
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; SM00490; HELICc; 1.
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 3: Inferred from homology;
KW ATP-binding; Cell membrane; Cytoplasm; Membrane; Metal-binding;
KW Nucleotide-binding; Protein transport; Reference proteome; Translocase;
KW Translocation; Transport; Zinc.
FT CHAIN 1..837
FT /note="Protein translocase subunit SecA 1"
FT /id="PRO_0000109590"
FT REGION 791..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..817
FT /note="Basic and acidic residues"
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 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 821
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 823
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 832
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 833
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT CONFLICT 95
FT /note="G -> D (in Ref. 1; AAA50286)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="I -> M (in Ref. 1; AAA50286)"
FT /evidence="ECO:0000305"
FT CONFLICT 439..442
FT /note="IETS -> MNI (in Ref. 1; AAA50286)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 837 AA; 94659 MW; 29F11A81980DBD02 CRC64;
MAGLLKKIFE SGKKDVKYLE RKADEIIALA DETAALSDDA LREKTVEFKE RVQKGETLDD
LLVEAFAVAR EGAKRALGLY PFKVQLMGGI VLHEGNIAEM KTGEGKTLTA TLPVYLNALS
GEGVHVVTVN EYLAHRDAEE MGVLYNFLGL SVGLNLNALS STEKREAYAC DITYSTNNEL
GFDYLRDNMV VYKEEMVQRP LAFAVIDEVD SILVDEARTP LIISGEAEKS TILYVRANTF
VRTLTEEEDY TVDIKTKSVQ LTEDGMTKGE NYFDVENLFD LENTVILHHI AQALKANYTM
SLDVDYVVQD DEVLIVDQFT GRIMKGRRFS EGLHQALEAK EGVTIQNESK TMATITFQNY
FRMYKKLAGM TGTAKTEEEE FRDIYNMRVI EIPTNKVIIR DDRPDLIYTT IEAKFNAVVE
DIAERHAKGQ PVLVGTVAIE TSELISSKLK RKGIKHDVLN AKQHEREADI IKHAGERGAV
VIATNMAGRG TDIKLGEGTI EAGGLAVIGT ERHESRRIDN QLRGRSGRQG DPGVTQFYLS
MEDELMRRFG SDNMKSMMER FGMAEDAIQS KMVSRAVESA QRRVEGNNFD SRKQVLQYDD
VLRQQREVIY KQRYEVINAE NSLREIIEQM IQRTVNFIVS SNASSHEPEE AWNLQGIIDY
VDANLLPEGT ITLEDLQNRT SEDIQNLILD KIKAAYDEKE TLLPPEEFNE FEKVVLLRVV
DTKWVDHIDA MDHLRDGIHL RAYGQIDPLR EYQSEGFEMF EAMVSSIDED VARYIMKAEI
RQNLEREQVA KGEAINPAEG KPEAKRQPIR KDQHIGRNDP CPCGSGKKYK NCHGKEA
