SECA2_BACAN
ID SECA2_BACAN Reviewed; 788 AA.
AC Q81UI7; Q6I2R6; Q6KWJ7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein translocase subunit SecA 2 {ECO:0000255|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA2 {ECO:0000255|HAMAP-Rule:MF_01382};
GN OrderedLocusNames=BA_0882, GBAA_0882, BAS0838;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(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 -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; AE016879; AAP24880.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT29993.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT53165.1; -; Genomic_DNA.
DR RefSeq; NP_843394.1; NC_003997.3.
DR RefSeq; WP_000935179.1; NZ_WXXJ01000017.1.
DR RefSeq; YP_027114.1; NC_005945.1.
DR AlphaFoldDB; Q81UI7; -.
DR SMR; Q81UI7; -.
DR IntAct; Q81UI7; 14.
DR STRING; 261594.GBAA_0882; -.
DR DNASU; 1088471; -.
DR EnsemblBacteria; AAP24880; AAP24880; BA_0882.
DR EnsemblBacteria; AAT29993; AAT29993; GBAA_0882.
DR GeneID; 45020946; -.
DR KEGG; ban:BA_0882; -.
DR KEGG; bar:GBAA_0882; -.
DR KEGG; bat:BAS0838; -.
DR PATRIC; fig|198094.11.peg.879; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_2_9; -.
DR OMA; IGQIHEF; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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; -; 3.
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; IPR030908; SecA2_Bac_anthr.
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 TIGRFAMs; TIGR04397; SecA2_Bac_anthr; 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..788
FT /note="Protein translocase subunit SecA 2"
FT /id="PRO_0000318311"
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 788 AA; 89537 MW; D413C0D5565BB863 CRC64;
MLNSVKKLLG DSQKRKLKKY EQLVQEINNL EEKLSDLSDE ELRHKTITFK DMLRDGKTVD
DIKVEAFAVV REAAKRVLGL RHYDVQLIGG LVLLEGNIAE MPTGEGKTLV SSLPTYVRAL
EGKGVHVITV NDYLAKRDKE LIGQVHEFLG LKVGLNIPQI DPSEKKLAYE ADITYGIGTE
FGFDYLRDNM AASKNEQVQR PYHFAIIDEI DSVLIDEAKT PLIIAGKKSS SSDLHYLCAK
VIKSFQDTLH YTYDAESKSA SFTEDGITKI EDLFDIDNLY DLEHQTLYHY MIQALRAHVA
FQCDVDYIVH DEKILLVDIF TGRVMDGRSL SDGLHQALEA KEGLEITEEN QTQASITIQN
FFRMYPALSG MTGTAKTEEK EFNRVYNMEV MPIPTNRPII REDKKDVVYV TADAKYKAVR
EDVLKHNKQG RPILIGTMSI LQSETVARYL DEANITYQLL NAKSAEQEAD LIATAGQKGQ
ITIATNMAGR GTDILLGEGV HELGGLHVIG TERHESRRVD NQLKGRAGRQ GDPGSSQFFL
SLEDEMLKRF AQEEVEKLTK SLKTDETGLI LTSKVHDFVN RTQLICEGSH FSMREYNLKL
DDVINDQRNV IYKLRNNLLQ EDTNMIEIII PMIDHAVEAI SKQYLVEGML PEEWDFASLT
ASLNEILSVE NMPSLSANNV HSPEDLQSVL KETLSLYKER VNELDSNTDL QQSLRYVALH
FLDQNWVNHL DAMTHLKEGI GLRQYQQEDP TRLYQKEALD IFLYTYGNFE KEMCRYVARH
LGVPENVQ
