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SECA_TRIL1
ID   SECA_TRIL1              Reviewed;         899 AA.
AC   B3E5W3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382};
DE            EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN   Name=secA {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=Glov_2490;
OS   Trichlorobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ) (Geobacter
OS   lovleyi).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Trichlorobacter.
OX   NCBI_TaxID=398767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1151 / DSM 17278 / SZ;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Sung Y., Fletcher K.E.,
RA   Ritalahti K.M., Loeffler F.E., Richardson P.;
RT   "Complete sequence of chromosome of Geobacter lovleyi SZ.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01382};
CC       Note=May bind 1 zinc ion per subunit. {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-YajC and YidC. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01382}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}.
CC       Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-
CC       50. {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; CP001089; ACD96204.1; -; Genomic_DNA.
DR   RefSeq; WP_012470537.1; NC_010814.1.
DR   AlphaFoldDB; B3E5W3; -.
DR   SMR; B3E5W3; -.
DR   STRING; 398767.Glov_2490; -.
DR   EnsemblBacteria; ACD96204; ACD96204; Glov_2490.
DR   KEGG; glo:Glov_2490; -.
DR   eggNOG; COG0653; Bacteria.
DR   HOGENOM; CLU_005314_3_0_7; -.
DR   OMA; MVHYDVQ; -.
DR   OrthoDB; 212453at2; -.
DR   Proteomes; UP000002420; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR004027; SEC_C_motif.
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; PF02810; SEC-C; 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 inner membrane; Cell membrane; Cytoplasm; Membrane;
KW   Metal-binding; Nucleotide-binding; Protein transport; Reference proteome;
KW   Translocase; Translocation; Transport; Zinc.
FT   CHAIN           1..899
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_1000145018"
FT   REGION          573..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          861..899
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         105..109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         512
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         885
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         887
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         896
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         897
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   899 AA;  102570 MW;  2208A263CC35620C CRC64;
     MLSTLIRKVI GSKNERELKR LWPIVAKINS LEPQMQALSD EELRGKTAEF KERYSKGESL
     DALLPEAFAV CREGGRRELG MRHFDVQLIG GMTLHAGKIA EMKTGEGKTL VATLAAYLNA
     ISGKGVHVVT VNDYLARRDS EWMGRLYGFL GLTTGVIVHG LDDEQRRANY AADITYGTNN
     EFGFDYLRDN MKFSLDDYVQ RGFNFAVVDE VDSILIDEAR TPLIISGPTE ESTDKYYVIN
     QIIPRLEQGE VKEVEANTLS GKKKVYTGDF TIDEKAKSAT LTEQGVSKVE KLLKIENLYD
     PRNIETLHHV NQALRAHAMY RRDVDYVVKD GEVLIVDEFT GRLMPGRRWS DGLHQAVEAK
     EGVRIESENQ TLATITFQNY FRMYAKLSGM TGTADTEAEE FHKIYKLDVT VIPTNRPLLR
     PDYPDVIYKT EQEKFAAVIS DIKEHYEKGQ PCLVGTISIE KSEVLSELLR KQGIPHFVLN
     AKQHEKEAEI VAQAGRKKAI TIATNMAGRG TDIVLGGNPD SLLKQWRLAN PEATAEQAAA
     MLEQYRQQCA AEHDEVVALG GLHIIGTERH ESRRIDNQLR GRSGRQGDPG SSRFYLSLQD
     DLLRIFGSER VAKIMDFLKI EEGEAITHAM INKSIENAQK KVEAHNFEIR KHLIDYDDVM
     NKQREVIYTQ RREILAGEDI RESFLEMLDD TISDIVKAYA FEKDAPLEWD WESLSETVFR
     CFSIQLELSR EMIARLNADG LQKMLQEQAH ESIKRRADEL GDELMDHLIR VVMLQAIDVH
     WKDHLLNIDH LKEGIGLRSY GQKDPKQEYK KEAYQLFMEM IIRIREETVE KVFWVQIEKE
     EDIEELEEEQ VERSRKMFKA ITVNDDEHPA EPAKSQKNAG RNEPCPCGSG KKYKKCCGK
 
 
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