SECA_SYNR3
ID SECA_SYNR3 Reviewed; 946 AA.
AC A5GQ30;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 89.
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};
GN OrderedLocusNames=SynRCC307_0086;
OS Synechococcus sp. (strain RCC307).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316278;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC307;
RG Genoscope;
RL Submitted (MAY-2006) 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 -!- FUNCTION: Probably participates in protein translocation into and
CC across both the cytoplasmic and thylakoid membranes in cyanobacterial
CC cells. {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 Cellular thylakoid 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}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK26989.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CT978603; CAK26989.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_043736384.1; NC_009482.1.
DR AlphaFoldDB; A5GQ30; -.
DR SMR; A5GQ30; -.
DR STRING; 316278.SynRCC307_0086; -.
DR EnsemblBacteria; CAK26989; CAK26989; SynRCC307_0086.
DR KEGG; syr:SynRCC307_0086; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_3; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000001115; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid 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; 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; Thylakoid;
KW Translocase; Translocation; Transport.
FT CHAIN 1..946
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000318473"
FT BINDING 90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 108..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 509
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 946 AA; 106899 MW; 13A96A4D4AAFCC39 CRC64;
MLKLLLGDPN ARKLKRYQPL VSDINLLEED IAPLSDEDLR RRTSEFRQQL ENAGSLERQR
PVLDQLLPEA FAIVREAGKR VLGMRHFDVQ LLGGMVLHDG QIAEMKTGEG KTLVATLPSY
LNALTGRGVH VVTVNDYLAR RDAEWMGQVH RFLGLSVGLI QQDMSPAERR QNYGCDVTYA
TNSELGFDYL RDNMATDISE VVQREFQYCV IDEVDSILVD EARTPLIISG QVERPQEKYN
QAAALALQLD RAAEMSKDGI DPEGDYEVDE KQRSVILTDE GYAKAESILG VEDLFNAADP
WAHYVTNALK AKELFIKDVN YITRDNEVVI VDEFTGRVMP GRRWSDGLHQ AVEAKESMPI
QPETQTLASI TYQNFFLLYP RLAGMTGTAK TEEVEFEKTY KLEVTVVPTN RTRARRDLVD
QVYKTETGKW RAVAQETAEV HRTGRPVLVG TTSVEKSEVL SALLQEEGIP HNLLNAKPEN
VEREAEIVAQ AGRTGAVTIA TNMAGRGTDI ILGGNTDYMA RLKVREALLP RLVRPEEGHR
PPVPLQREAS SGFAAAASAP AKPPSEARAL GRLYPCELSP DTDAALADVA RELVKLWGDR
TLTVLELEDR ISSAAEKAPS EDAGIMQLRQ VLAQIRADYD AVISTEQASV RETGGLHVIG
TERHESRRVD NQLRGRAGRQ GDPGSTRFFL SLEDNLLRIF GGDRVAGLMN AFRVEEDMPI
ESGMLTRSLE GAQKKVETYY YDMRKQVFEY DEVMNNQRRA VYVERRRVLE GRDLKKQVLG
YGERTMDDIV EAYVNPELPP EEWDLSHLTN KVKEFVYLLQ DLEPQQLAGL SMEELKAFLH
EQLRIAYDLK EAEIEQLKPG LMREAERFFI LQQIDSLWRE HLQSMDALRE SVGLRGYGQK
DPLIEYKNEG YDMFLEMMTQ VRRNVIYSMF MFQPQPAPAQ EDEAVV
