SECA1_MYCPA
ID SECA1_MYCPA Reviewed; 940 AA.
AC Q73UL2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=MAP_3354c;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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 -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; AE016958; AAS05904.1; -; Genomic_DNA.
DR RefSeq; WP_010949934.1; NC_002944.2.
DR AlphaFoldDB; Q73UL2; -.
DR SMR; Q73UL2; -.
DR STRING; 262316.MAP_3354c; -.
DR EnsemblBacteria; AAS05904; AAS05904; MAP_3354c.
DR KEGG; mpa:MAP_3354c; -.
DR PATRIC; fig|262316.17.peg.3564; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_11; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000000580; 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: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; 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; PS51196; SECA_MOTOR_DEAD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW Protein transport; Reference proteome; Translocase; Translocation;
KW Transport.
FT CHAIN 1..940
FT /note="Protein translocase subunit SecA 1"
FT /id="PRO_0000318380"
FT REGION 856..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 101..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 490
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 940 AA; 105244 MW; 50CCE6B3E74A1E5A CRC64;
MLSKLLRLGE GRMLKRLKRV ADYVNTLSDE VEKLTDAELR AKTDEFKKRH ADGESLDDLL
PEAFAVAREA AWRVLDQRPF DVQVMGAAAL HFGNVAEMKT GEGKTLTSVL PAYLNGIGGK
GVHVVTVNDY LAKRDSEWMG RVHRFLGLDV GVILAQMTPD ERRVAYNADI TYGTNNEFGF
DYLRDNMAHS LDDLVQRGHN FAIVDEVDSI LIDEARTPLI ISGPADGASN WYLEFARLAP
LMEKDVHYEV DLRKRTVGVH ELGVEFVEDQ LGIDNLYEAA NSPLVSYLNN ALKAKELFHR
DKDYIVRDGE VLIVDEFTGR VLYGRRYNEG MHQAIEAKEH VEIKAENQTL ATITLQNYFR
LYDKLSGMTG TAQTEAAELH EIYKLGVVPI PTNKPMIRTD QSDLIYKTEE AKYIAVVDDV
VERYQKGQPV LIGTTSVERS EYLSRQFQKR RIPHNVLNAK YHEQEAGIVA VAGRRGGVTV
ATHMAGRGTD IVLGGNVDFL TDQRLRERGL DPVETPDEYE AAWHEELPKV KAEAAAEAKE
VIEAGGLYVL GTERHESRRI DNQLRGRSGR QGDPGESRFY LSLGDELMRR FNGAALEAML
NRLNLPDDVP IEAKMVTRAI KSAQTQVEQQ NFEVRKNVLK YDEVMNQQRK VIYAERRRIL
EGENLKEQAL EMVRDVVTAY VNGATAEGYA EDWDLDALWT ALKTLYPVGI DYATLTRRDA
DGGFDDLTRE ELLEALLKDA ERAYATREAE LEEIAGEGAM RQLERNVLLN VIDRKWREHL
YEMDYLKEGI GLRAMAQRDP LVEYQREGYD MFMAMLDGMK EESVGFLFNV TVEAVPAPQV
APVQTPEGLA ELGAPAEQGG TATAARDEAP TQLRAKGIDN EAPAMTYSGP SEDGSAQVQR
NGGDAKTPAG VPAGASRRER RAAARQQGRG AKPPKSVKRR
