SECA1_MYCLE
ID SECA1_MYCLE Reviewed; 940 AA.
AC P57996;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=ML0779;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(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 -!- 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; AL583919; CAC30288.1; -; Genomic_DNA.
DR PIR; D87006; D87006.
DR RefSeq; NP_301603.1; NC_002677.1.
DR RefSeq; WP_010907927.1; NC_002677.1.
DR AlphaFoldDB; P57996; -.
DR SMR; P57996; -.
DR STRING; 272631.ML0779; -.
DR EnsemblBacteria; CAC30288; CAC30288; CAC30288.
DR KEGG; mle:ML0779; -.
DR PATRIC; fig|272631.5.peg.1398; -.
DR Leproma; ML0779; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_11; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000000806; 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; Reference proteome; Translocase; Translocation;
KW Transport.
FT CHAIN 1..940
FT /note="Protein translocase subunit SecA 1"
FT /id="PRO_0000109594"
FT REGION 867..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..940
FT /note="Basic 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"
SQ SEQUENCE 940 AA; 105528 MW; 00AAEBF62D76DD71 CRC64;
MLSKLLRLGE GRIVKRLKRV AEYVNTLSDN VEKLTDVELK AKTDEFKQRL ADEKNPESLD
DLLPEAFAVA REAAWRVLDQ RPFDVQVMGG AALHLGNVAE MKTGEGKTLT CVLPAYLNAL
AGKGVHIVTV NDYLAKRDSE WMGRVHRFLG LQVGVILASM TPDERRVAYN ADITYGTNNE
FGFDYLRDNM AHSLDDLVQR GHSYAIVDEV DSILIDEART PLIISGSADG ASNWYTEFAR
LVRLMDKDVH YEVDLRKRTV GVHEKGMEFV EDQLGIDNLY EVANSPLVSY LNNALKAKEL
FNRDKDYIVR DGEVLIVDEF TGRVLIGRRY NEGMHQAIEA KEHVEIKAEN QTLATITLQN
YFRLYDKLAG MTGTAQTEAA ELHEIYKLGV VAIPTNKPMI REDRSDLIYK TEEAKYMAVV
DDVAERYEKG QPVLIGTTSV ERSEYLSRQF TKRHIPHNVL NAKYHEQEAG IVAVAGRRGG
VTVATNMAGR GTDIVLGGNV DFLTDQRLRR RGLDPVETPD EYEQAWHSEL PKVKEEAGQE
AAEVIEAGGL YVLGTERHES RRIDNQLRGR SGRQGDPGES RFYLSLGDEL MRRFHGATLE
ALLTRLNLPD DVPIEAKMVT RAIKSAQTQV EQQNFEVRKN VLKYDEVMNQ QRKVIYAERR
RILEGESLQQ QALGMVRDVI TAYIDGATTD SYVEDWDLDA LWSALGTLYP VGIKHESLTH
ADEDSECDEL SRDELLEALL IDAQHAYAAR EAELAELAGE GAMRQLERNV LLNVVDRKWR
EHLYEMDYLK EGIGLRAMAQ RDPLVEYQRE GYDMFMAMLD GVKEESVGFL FNLAVEAVPA
SHVAPVEIPE GFTGLVADVE AIRPREEASS ALRTKDIDNE STGLTYSGPS EDGSTQVQLN
SGGGQKTPAG IPVGASRRER REAARRRGRG AKPSRSVKKR
