SECA_NOSS1
ID SECA_NOSS1 Reviewed; 930 AA.
AC Q8YMS8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=alr4851;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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; BA000019; BAB76550.1; -; Genomic_DNA.
DR PIR; AC2412; AC2412.
DR RefSeq; WP_010998979.1; NZ_RSCN01000037.1.
DR AlphaFoldDB; Q8YMS8; -.
DR SMR; Q8YMS8; -.
DR STRING; 103690.17133988; -.
DR EnsemblBacteria; BAB76550; BAB76550; BAB76550.
DR KEGG; ana:alr4851; -.
DR eggNOG; COG0653; Bacteria.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000002483; 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..930
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000318305"
FT BINDING 83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 101..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 491
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 930 AA; 106130 MW; 0049637AA84CF065 CRC64;
MLKLLLGDPN ARKLKKYQPY ITEINLLEED IKVLSDEDLK GKTAEFKQRL AKGETLDDIL
PEAFAVVREA GRRVLGLRHF DVQMLGGVIL HSGQIAEMKT GEGKTLVATL PSYLNALTGK
GVHVITVNDY LARRDAEWMG QVHRFLGLSV GLIQSSMTPS ERQKNYECDI TYVTNSEVGF
DYLRDNMATS MADVVQRPFN YCVIDEVDSI LVDEARTPLI ISGQVERPTE KYVQAAEIAL
TLQKDEHYDV DEKARNVLLT DEGFAQAEEL LGVTDLFDPE DPWAHFVFNA IKAKELFLKD
VNYIVRNGEV VIVDEFTGRV LPGRRWSDGL HQAIEAKEHV DIQPETQTLA TITYQNLFLL
YPKLGGMTGT AKTEEAEFER IYKLEVTIIP TNRIRRREDL SDLVFKKEIG KWQAIARECA
EMHELGRPVL VGTTSVEKSE YLSQLLREQG IPHELLNARP ENVEREAEIV AQAGRRGAVT
IATNMAGRGT DIILGGNSEY MARLKLREYF MPRIVRPDDE DVFGVQRAAG LPTGHGAGQG
FVPGKKVKTW KASPEIFPTQ LSKEAEQLLK EAVDFAVREY GDRSLPELEA EDKVAVAAEK
APTDDSVIQK LRDAYNRIKH EYEEFTSTEH DEVVGRGGLH VIGTERHESR RIDNQLRGRA
GRQGDPGSTR FFLSLEDNLL RIFGGDRVAG LMEAFNVEDD MPIESGMLTR SLEGAQRKVE
TYYYDIRKQV FEYDEVMNNQ RRAIYAERRR VLEGQDLKEQ VIKYAEKTMD EIVDYYINVD
LPSEEWELDK LVDKVKEFVY LLSDMQANQL EDMGVSEIKA FLHEQVRIAY DLKEAQIDQI
QPGLMRQAER FFILQRIDTL WREHLQQMDA LRESVGLRGY GQKDPLIEYK SEGYELFLDM
MVNIRRDVVY SLFMFQPQPQ PVVQTSSEMV
