SECA_CYAP4
ID SECA_CYAP4 Reviewed; 932 AA.
AC B8HSJ5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=Cyan7425_3658;
OS Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Cyanothecaceae; Cyanothece; unclassified Cyanothece.
OX NCBI_TaxID=395961;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7425 / ATCC 29141;
RX PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
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; CP001344; ACL45978.1; -; Genomic_DNA.
DR RefSeq; WP_012629036.1; NC_011884.1.
DR AlphaFoldDB; B8HSJ5; -.
DR SMR; B8HSJ5; -.
DR STRING; 395961.Cyan7425_3658; -.
DR PRIDE; B8HSJ5; -.
DR EnsemblBacteria; ACL45978; ACL45978; Cyan7425_3658.
DR KEGG; cyn:Cyan7425_3658; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_3; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
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..932
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000184224"
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 932 AA; 106141 MW; 691786CF95EFCEBF CRC64;
MLKTLLGDPN KRKLKKYQPD VVEINLLEPE MQALSDQELQ SKTGEFKRQL EQGKSLDELL
PEAFAVVREA SRRVLGLRHF DVQLLGGMIL HDGQIAEMKT GEGKTLVSTL PAYLNALTGK
GVQIITVNDY LARRDAEWMG QVHRFLGLSV GLIQQSMPPQ ERQKNYACDI TYATNSEIGF
DYLRDNMATS MAEVVLRPFH YCVIDEVDSV LIDEARTPLI ISGQVERPTE KYLRATAIAD
ALQKEEHYEV DEKARNILLT DEGFIEAEKL LGVKDLFDSQ DPWAHYIFNA VKAKELFIKD
VNYIIRGGEI VIVDEFTGRV MPGRRWSDGL HQAIEAKEGL DIQNESQTLA TITYQNLFLL
YPKLAGMTGT AKTEEAEFEK IYKLEVTVVP TNRATGRRDL PDVVYKNEMA KWRAVAAECA
EFHQAGRPVL VGTTSVEKSE VLSQLLNQAG IPHNLLNAKP ENVERESEIV AQAGRKGAVT
IATNMAGRGT DIILGGNADY MARLKVREYF MPRIVMPESD DPLAMMRIMM GDGNASGGQG
FAPQGNRPQK TWKASPNIFP TKLSRETEQL LKAAVDFAVK QYGERSIPEL QAEDIVAIAS
EKAPTEDPVV QRLREAYNQI RSEYETFTHQ EHDEVVQFGG LHVIGTERHE SRRVDNQLRG
RAGRQGDPGS TRFFLSLEDN LLRIFGGDRV AGLMNAFRVE EDMPIESRIL TGSLENAQRK
VETYYYDIRK QVFEYDDVMN NQRRAIYAER RRVLEGEDLK ERVLEYAERT MDDIVEAYVN
PDLPPEEWDL NSMVGKVKEF VNLLADLEPQ QLEDLSMAEM QMFLHEQVRI AYDRKEAEID
QLQPGLMRQA ERFFILQQID TLWREHLQAM DALRESVGLR GYGQQDPLVE YKSEGYELFL
DMMTAIRRNV VYSLFQFQPQ YQPPEEMPSE VV
