SECA1_MYCS2
ID SECA1_MYCS2 Reviewed; 953 AA.
AC P71533; A0QTK8; I7FYZ8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 139.
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=MSMEG_1881, MSMEI_1840;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=11717254; DOI=10.1128/jb.183.24.6979-6990.2001;
RA Braunstein M., Brown A.M., Kurtz S., Jacobs W.R. Jr.;
RT "Two nonredundant SecA homologues function in mycobacteria.";
RL J. Bacteriol. 183:6979-6990(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(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 -!- 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 -!- DISRUPTION PHENOTYPE: Essential, it cannot be disrupted.
CC {ECO:0000269|PubMed:11717254}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; U66081; AAB06754.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK74020.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP38312.1; -; Genomic_DNA.
DR RefSeq; WP_011727975.1; NZ_SIJM01000020.1.
DR RefSeq; YP_886246.1; NC_008596.1.
DR AlphaFoldDB; P71533; -.
DR SMR; P71533; -.
DR STRING; 246196.MSMEI_1840; -.
DR PRIDE; P71533; -.
DR EnsemblBacteria; ABK74020; ABK74020; MSMEG_1881.
DR EnsemblBacteria; AFP38312; AFP38312; MSMEI_1840.
DR GeneID; 66733315; -.
DR KEGG; msg:MSMEI_1840; -.
DR KEGG; msm:MSMEG_1881; -.
DR PATRIC; fig|246196.19.peg.1862; -.
DR eggNOG; COG0653; Bacteria.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR BRENDA; 7.4.2.5; 3445.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW Protein transport; Reference proteome; Translocase; Translocation;
KW Transport.
FT CHAIN 1..953
FT /note="Protein translocase subunit SecA 1"
FT /id="PRO_0000109597"
FT REGION 854..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..943
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"
FT CONFLICT 260
FT /note="H -> HVGVH (in Ref. 1; AAB06754)"
FT /evidence="ECO:0000305"
FT CONFLICT 752
FT /note="E -> K (in Ref. 1; AAB06754)"
FT /evidence="ECO:0000305"
FT CONFLICT 775
FT /note="K -> Q (in Ref. 1; AAB06754)"
FT /evidence="ECO:0000305"
FT CONFLICT 908..909
FT /note="DG -> ER (in Ref. 1; AAB06754)"
FT /evidence="ECO:0000305"
FT CONFLICT 912
FT /note="Q -> H (in Ref. 1; AAB06754)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 953 AA; 106488 MW; 4D1AB93BC0752221 CRC64;
MLSKLLRLGE GRMVKRLRKV ADYVNALSDD VEKLSDAELR AKTEEFKKRV ADGEDLDDLL
PEAFAVAREA AWRVLNQRHF DVQVMGGAAL HFGNVAEMKT GEGKTLTAVL PSYLNALSGK
GVHVVTVNDY LARRDSEWMG RVHRFLGLDV GVILSGMTPD ERRAAYAADI TYGTNNEFGF
DYLRDNMAHS VDDMVQRGHN FAIVDEVDSI LIDEARTPLI ISGPADGASH WYQEFARIVP
MMEKDVHYEV DLRKRTVGVH ELGVEFVEDQ LGIDNLYEAA NSPLVSYLNN ALKAKELFQR
DKDYIVRNGE VLIVDEFTGR VLMGRRYNEG MHQAIEAKER VEIKAENQTL ATITLQNYFR
LYDKLSGMTG TAETEAAELH EIYKLGVVPI PTNKPMVRQD QSDLIYKTEE AKFLAVVDDV
AERHAKGQPV LIGTTSVERS EYLSKMLTKR RVPHNVLNAK YHEQEANIIA EAGRRGAVTV
ATNMAGRGTD IVLGGNVDFL ADKRLRERGL DPVETPEEYE AAWHEVLPQV KAECAKEAEQ
VIEAGGLYVL GTERHESRRI DNQLRGRSGR QGDPGESRFY LSLGDELMRR FNGATLETLL
TRLNLPDDVP IEAKMVSRAI KSAQTQVEQQ NFEVRKNVLK YDEVMNQQRK VIYAERRRIL
EGENLAEQAH KMLVDVITAY VDGATAEGYA EDWDLETLWT ALKTLYPVGI DHRDLIDSDA
VGEPGELTRE ELLDALIKDA ERAYAEREKQ IEAIAGEGAM RQLERNVLLN VIDRKWREHL
YEMDYLKEGI GLRAMAQRDP LVEYQREGYD MFVGMLEALK EESVGFLFNV QVEAAPQQPQ
VAPQAPPPTL SEFAAAAAAK ASDSAAKPDS GSVATKERAE AERPAPALRA KGIDNEAPPL
TYTGPSEDGT AQVQRSGNGG RHAAPAGGSR RERREAARKQ AKADRPAKSH RKG
