SECA1_MYCBO
ID SECA1_MYCBO Reviewed; 949 AA.
AC P0A5Y9; A0A1R3Y3Q2; O05885; P71494; X2BNE8;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=BQ2027_MB3268C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF THR-129.
RC STRAIN=BCG;
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 BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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; U66080; AAC34131.1; -; Genomic_DNA.
DR EMBL; LT708304; SIU01897.1; -; Genomic_DNA.
DR RefSeq; NP_856913.1; NC_002945.3.
DR RefSeq; WP_003901576.1; NC_002945.4.
DR AlphaFoldDB; P0A5Y9; -.
DR SMR; P0A5Y9; -.
DR EnsemblBacteria; SIU01897; SIU01897; BQ2027_MB3268C.
DR GeneID; 45427234; -.
DR PATRIC; fig|233413.5.peg.3595; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000001419; 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; Translocase; Translocation; Transport.
FT CHAIN 1..949
FT /note="Protein translocase subunit SecA 1"
FT /id="PRO_0000109591"
FT REGION 869..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..938
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 104..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT MUTAGEN 129
FT /note="T->I: Azide resistant."
FT /evidence="ECO:0000269|PubMed:11717254"
FT CONFLICT 231..239
FT /note="ASNWYTEFA -> LQLVHRVR (in Ref. 1; AAC34131)"
FT /evidence="ECO:0000305"
FT CONFLICT 334..335
FT /note="MH -> ID (in Ref. 1; AAC34131)"
FT /evidence="ECO:0000305"
FT CONFLICT 711
FT /note="V -> E (in Ref. 1; AAC34131)"
FT /evidence="ECO:0000305"
FT CONFLICT 800..801
FT /note="QR -> HG (in Ref. 1; AAC34131)"
FT /evidence="ECO:0000305"
FT CONFLICT 932
FT /note="A -> R (in Ref. 1; AAC34131)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 949 AA; 106022 MW; D46C3315835E03D7 CRC64;
MLSKLLRLGE GRMVKRLKKV ADYVGTLSDD VEKLTDAELR AKTDEFKRRL ADQKNPETLD
DLLPEAFAVA REAAWRVLDQ RPFDVQVMGA AALHLGNVAE MKTGEGKTLT CVLPAYLNAL
AGNGVHIVTV NDYLAKRDSE WMGRVHRFLG LQVGVILATM TPDERRVAYN ADITYGTNNE
FGFDYLRDNM AHSLDDLVQR GHHYAIVDEV DSILIDEART PLIISGPADG ASNWYTEFAR
LAPLMEKDVH YEVDLRKRTV GVHEKGVEFV EDQLGIDNLY EAANSPLVSY LNNALKAKEL
FSRDKDYIVR DGEVLIVDEF TGRVLIGRRY NEGMHQAIEA KEHVEIKAEN QTLATITLQN
YFRLYDKLAG MTGTAQTEAA ELHEIYKLGV VSIPTNMPMI REDQSDLIYK TEEAKYIAVV
DDVAERYAKG QPVLIGTTSV ERSEYLSRQF TKRRIPHNVL NAKYHEQEAT IIAVAGRRGG
VTVATNMAGR GTDIVLGGNV DFLTDQRLRE RGLDPVETPE EYEAAWHSEL PIVKEEASKE
AKEVIEAGGL YVLGTERHES RRIDNQLRGR SGRQGDPGES RFYLSLGDEL MRRFNGAALE
TLLTRLNLPD DVPIEAKMVT RAIKSAQTQV EQQNFEVRKN VLKYDEVMNQ QRKVIYAERR
RILEGENLKD QALDMVRDVI TAYVDGATGE GYAEDWDLDA LWTALKTLYP VGITADSLTR
KDHEFERDDL TREELLEALL KDAERAYAAR EAELEEIAGE GAMRQLERNV LLNVIDRKWR
EHLYEMDYLK EGIGLRAMAQ RDPLVEYQRE GYDMFMAMLD GMKEESVGFL FNVTVEAVPA
PPVAPAAEPA ELAEFAAAAA AAAQQRSAVD GGARERAPSA LRAKGVASES PALTYSGPAE
DGSAQVQRNG GGAHKTPAGV PAGASRRERR EAARRQGRGA KPPKSVKKR
