SECA_SYNP6
ID SECA_SYNP6 Reviewed; 948 AA.
AC Q5N2Q7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=syc1223_c;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
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}.
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DR EMBL; AP008231; BAD79413.1; -; Genomic_DNA.
DR RefSeq; WP_011243535.1; NC_006576.1.
DR AlphaFoldDB; Q5N2Q7; -.
DR SMR; Q5N2Q7; -.
DR STRING; 269084.syc1223_c; -.
DR TCDB; 3.A.5.4.1; the general secretory pathway (sec) family.
DR EnsemblBacteria; BAD79413; BAD79413; syc1223_c.
DR KEGG; syc:syc1223_c; -.
DR eggNOG; COG0653; Bacteria.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000001175; 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; Thylakoid; Translocase;
KW Translocation; Transport.
FT CHAIN 1..948
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000318467"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 109..113
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 948 AA; 107258 MW; B6A90238B9BFC656 CRC64;
MLNLLLGDPN VRKVKKYKPL VTEINLLEED IEPLSDKDLI AKTAEFRQKL DKVSHSPAAE
KELLAELLPE AFAVMREASK RVLGLRHFDV QMIGGMILHD GQIAEMKTGE GKTLVATLPS
YLNALSGKGA HVVTVNDYLA RRDAEWMGQV HRFLGLSVGL IQQGMSPEER RRNYNCDITY
ATNSELGFDY LRDNMAAVIE EVVQRPFNYA VIDEVDSILI DEARTPLIIS GQVDRPSEKY
MRASEVAALL QRSTNTDSEE EPDGDYEVDE KGRNVLLTDQ GFINAEQLLG VSDLFDSNDP
WAHYIFNAIK AKELFIKDVN YIVRGGEIVI VDEFTGRVMP GRRWSDGLHQ AVESKEGVEI
QPETQTLASI TYQNFFLLYP KLSGMTGTAK TEELEFEKTY KLEVTVVPTN RVSRRRDQPD
VVYKTEIGKW RAIAADCAEL HAEGRPVLVG TTSVEKSEFL SQLLNEQGIP HNLLNAKPEN
VEREAEIVAQ AGRRGAVTIS TNMAGRGTDI ILGGNADYMA RLKLREYWMP QLVSFEEDGF
GIAGVAGLEG GRPAAQGFGS PNGQKPRKTW KASSDIFPAE LSTEAEKLLK AAVDLGVKTY
GGNSLSELVA EDKIATAAEK APTDDPVIQK LREAYQQVRK EYEAVTKQEQ AEVVELGGLH
VIGTERHESR RVDNQLRGRA GRQGDPGSTR FFLSLEDNLL RIFGGDRVAK LMNAFRVEED
MPIESGMLTR SLEGAQKKVE TYYYDIRKQV FEYDEVMNNQ RRAIYAERRR VLEGRELKEQ
VIQYGERTMD EIVDAHINVD LPSEEWDLEK LVNKVKQFVY LLEDLEAKQL EDLSPEAIKI
FLHEQLRIAY DLKEAQIDQI QPGLMRQAER YFILQQIDTL WREHLQAMEA LRESVGLRGY
GQKDPLLEYK SEGYELFLEM MTAIRRNVIY SMFMFDPQPQ ARPQAEVV
