SECA_GLOVI
ID SECA_GLOVI Reviewed; 952 AA.
AC Q7NJJ6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=gll1836;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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 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; BA000045; BAC89777.1; -; Genomic_DNA.
DR RefSeq; NP_924782.1; NC_005125.1.
DR RefSeq; WP_011141834.1; NC_005125.1.
DR AlphaFoldDB; Q7NJJ6; -.
DR SMR; Q7NJJ6; -.
DR STRING; 251221.35212402; -.
DR EnsemblBacteria; BAC89777; BAC89777; BAC89777.
DR KEGG; gvi:gll1836; -.
DR PATRIC; fig|251221.4.peg.1867; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_3; -.
DR InParanoid; Q7NJJ6; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR PhylomeDB; Q7NJJ6; -.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015462; F:ABC-type protein transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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 GO; GO:0043952; P:protein transport by the Sec complex; IBA:GO_Central.
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; 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 inner membrane; Cell membrane; Cytoplasm; Membrane;
KW Nucleotide-binding; Protein transport; Reference proteome; Translocase;
KW Translocation; Transport.
FT CHAIN 1..952
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000318361"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 122..126
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"
SQ SEQUENCE 952 AA; 107740 MW; 0F08901EBFCEF934 CRC64;
MAWWNKLFGD PQERKVKKYQ PRVAEMNALE AEVAALSDDQ LRAKTAVFQK RVADQLQGVD
LDALEIRERR RRIDVALDGV ISEAFAVVRE AAKRVIGLRH YDVQLIGGLV LHEGQIAEMK
TGEGKTLVAT LPAYLNALTG RGVHIVTVND YLARRDSEWM GQVHRFLGLS VGLIQQSMTP
SERAQNYAAD ITYGTNSELG FDYLRDNMAT NAGELVQRSF NYCIIDEVDS ILVDEARTPL
IISGMVAKPA EKYMRANEVA TALERNTHYE VDEKQRNVTL TDEGFIAAEQ MLSTEDLFSP
RDPWAHFVFN AVKAKELFNK DVQYIVRNDE VVIVDEFTGR VMPGRRWSEG LHQAVEAKEM
VTIQNETQTM ASITYQNFFL LYPKLAGMTG TALTEEAEFG KIYSLEVTAI PTNRKVVRTD
MSDQVYKTEN GKWQSVAAEI AEMNKNGRPV LVGTTSVEKS EVLSALLKEK GIAHNLLNAK
PENVERESEI VAQAGRKGGV TIATNMAGRG TDILLGGNPE YMARLKLKEV LFPALVIDDE
DAFSPMMRLL NNGNSRGTGF AATSKKKALP KAEIFPCELS ESTKQQLKAA VDYAVAMLGA
DSQPALQVEE LIAVASEKGP TDDPVIQHLR EIYRAIYKEY QVVTDREHDE VVKLGGLHVI
GTERHEARRV DNQLRGRSGR QGDPGSTRFF LSLGDNLLRI FGGERVAGLM EAFKVEEDMP
IESGLLTKSL ENAQRKVETF YYDQRKQVFE YDEVMNNQRK AIYAERRRAL EGQDLSAVVR
EYIDQTVDEI VRAHVNAERP PEEWELPALI QDLQQLIPLL ENQLDAVKLG EFSAVELEED
LKSQALLAYE TREEYINAIQ PDLMREAERY FILNQIDTLW REHLQQMDSL REMIGLRGYG
QKDPLIEYKN EGYELFLQML VEVRRNVVFA LYHFQPQYNP PIDPDYVDSE YV
