SECA1_MYCUA
ID SECA1_MYCUA Reviewed; 950 AA.
AC A0PRE5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=MUL_2576;
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=362242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99;
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
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; CP000325; ABL04914.1; -; Genomic_DNA.
DR RefSeq; WP_011740529.1; NC_008611.1.
DR AlphaFoldDB; A0PRE5; -.
DR SMR; A0PRE5; -.
DR STRING; 362242.MUL_2576; -.
DR EnsemblBacteria; ABL04914; ABL04914; MUL_2576.
DR KEGG; mul:MUL_2576; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_11; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000000765; 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; 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 3: Inferred from homology;
KW ATP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW Protein transport; Translocase; Translocation; Transport.
FT CHAIN 1..950
FT /note="Protein translocase subunit SecA 1"
FT /id="PRO_0000318392"
FT REGION 864..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..939
FT /note="Basic and acidic residues"
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 950 AA; 106326 MW; D33DFA452B801CBE CRC64;
MLSKLLRVGE GRMVKRLKKV ADYVESLSGD VEKLTDAELR AKTDEFKKRH AEGESLDELL
PEAFAVAREA AWRVLGQRPF EVQLMGAAAL HLGNVAEMKT GEGKTLTSVL PAYLNGIGGK
GVHIVTVNDY LAKRDSEWMG RVHRFLGLDV GVILAQMTPE ERRVAYNADI TYGTNNEFGF
DYLRDNMAHT LDDCVQRGHN FVIVDEVDSI LIDEARTPLI ISGPADGSSN WYTEFARLAP
LMEKDTHYEV DLRKRTVGVH ELGVEFVEDQ LGIDNLYEAA NSPLVSYLNN ALKAKELFNR
DKDYIVRNGE VLIVDEFTGR VLIGRRYSEG MHQAIEAKEH VEIKAENQTL ATITLQNYFR
LYNKHAGMTG TAQTEAAELH EIYKLGVVPI PTNRPMVRED QSDLIYKTEE AKYIAVVDDV
AERYEKGQPV LIGTTSVERS EYLSRQFTKR RIPHNVLNAK YHEQEAGIIA EAGRRGAITV
ATNMAGRGTD IVLGGNVDFL TDKRLRDNGL DPVETPDEYE QAWHQELPKV KEEAGDEATE
VIKAGGLYVL GTERHESRRI DNQLRGRSGR QGDPGESRFY LSLGDELMRR FNGAALESLL
TRLNLPDDVP IEAKMVTRAI KSAQTQVEQQ NFEVRKNVLK YDEVMNQQRK VIYAERRRIL
EGENLQQQVK DMLTDVITAY VDGATVEGYA EDWDLDALWT ALKTLYPVGI KTDTLMRRDQ
DSDRDDLTRD ELLQALLQDA DQAYAAREAE LEELAGEGAM RQLERNVLLN VIDRKWREHL
YEMDYLKEGI GLRAMAQRDP LVEYQREGYD MFMAMLDGVK EESVGFLFNV SVEAVPAPQV
EVAPVAEPED LAEFATAAAA AAQEGGAGRK NAAAREEAPS RLRAKGIEDE SPALTYSGPS
EDGSAQVQRN GGGAAKTPAG VPAGRSRRER REAARRQGRG AKPPKSVKKR
