SECA_SYNPW
ID SECA_SYNPW Reviewed; 955 AA.
AC A5GI02;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=SynWH7803_0141;
OS Synechococcus sp. (strain WH7803).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32051;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7803;
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}.
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DR EMBL; CT971583; CAK22567.1; -; Genomic_DNA.
DR RefSeq; WP_011932075.1; NC_009481.1.
DR AlphaFoldDB; A5GI02; -.
DR SMR; A5GI02; -.
DR STRING; 32051.SynWH7803_0141; -.
DR EnsemblBacteria; CAK22567; CAK22567; SynWH7803_0141.
DR KEGG; syx:SynWH7803_0141; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_3; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000001566; 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..955
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000318474"
FT REGION 537..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 955 AA; 107285 MW; 19D511E342EA7773 CRC64;
MLKLLLGDPN ARKLKRYQPI VSDINLLEEE VSPLSDDDLR RRTAEFRQRL DNAGSLDQQR
PVLDELLPEA FAVVREAGKR VLGMRHFDVQ LIGGMVLHEG QIAEMKTGEG KTLVATLPSF
LNALTGRGVH VVTVNDYLAR RDAEWMGQVH RFLGLSVGLI QQDMTPAERR RNYGCDITYA
TNSELGFDYL RDNMAADINE VVQREFQYCV IDEVDSILID EARTPLIISG QVERPQEKYQ
KAAEVAAALT RAAEMGKDGI DPEGDYEVDE KQRSCTLTDE GFAKAEQMIG VADLYDPQDP
WAHYITNALK AKDLFTRDVN YIVRDGEAVI VDEFTGRVMP GRRWSDGQHQ AIEAKEALAI
QPETQTLASI TYQNFFLLYP RLAGMTGTAK TEETEFEKTY KLETTIVPTN RVRARQDWVD
QVYKTEEAKW RAVAKETAEV HQQGRPVLVG TTSVEKSELL SALLAEEDIP HNLLNAKPEN
VEREAEIVAQ AGRSGAVTIA TNMAGRGTDI ILGGNSDYMA RLKLREVLLS RLVRPEEGHR
PPVPLQRSGA EGGGGFAAKA APASGPHGHA PSEARAIGSL YPCQLTEDTD QALADLAKDL
VKAWGDRALT VIELEDHIAT AAEKAPTDDP AIAALRAAIA RVKGEYDDVV KQEEQRVREA
GGLHVIGTER HESRRVDNQL RGRAGRQGDP GSTRFFLSLG DNLLRIFGGD RVAGLMNAFR
VEEDMPIESG MLTRSLEGAQ KKVETYYYDI RKQVFEYDEV MNNQRKAVYS ERRRVLEGRE
LKKQVVGYGE RTMNEIVEAY VNPDLPPEEW DVTQLVSKVQ EFVYLLDDLQ ADQLQGLSMD
ELKAFLQEQL RNAYDLKEGQ IEDQRPGLMR EAERFFILQQ IDTLWREHLQ SMDALRESVG
LRGYGQKDPL IEYKNEGYDM FLDMMTNMRR NVIYSMFMFQ PAPPAGQSAG QRTTA
