SECA_SYNSC
ID SECA_SYNSC Reviewed; 934 AA.
AC Q3ANH2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=Syncc9605_0081;
OS Synechococcus sp. (strain CC9605).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=110662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9605;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9605.";
RL Submitted (JUL-2005) 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; CP000110; ABB33860.1; -; Genomic_DNA.
DR RefSeq; WP_011363120.1; NC_007516.1.
DR AlphaFoldDB; Q3ANH2; -.
DR SMR; Q3ANH2; -.
DR STRING; 110662.Syncc9605_0081; -.
DR EnsemblBacteria; ABB33860; ABB33860; Syncc9605_0081.
DR KEGG; syd:Syncc9605_0081; -.
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..934
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000318469"
FT REGION 535..565
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 934 AA; 105317 MW; 4DAE994CF1BB0575 CRC64;
MLKLLLGDPN ARKLKRYQPI VSDIQLLEEE IAPLSDDELR GRTAAFQERL ANAGSLANQR
PILDEILPEA FAVVREAGKR VLGMRHFDVQ LIGGMVLHEG QIAEMKTGEG KTLVATLPSY
LNALTGRGVH VVTVNDYLAR RDAEWMGQVH RFLGLSVGLI QQDMRPEERR RNYNCDITYA
TNSELGFDYL RDNMAADISE VVQREFQYCV IDEVDSILID EARTPLIISG QVERPQEKYQ
QAAEVANALA RAAELSKDGI DPEGDYEVDE KQRSCTLTDE GFAKAEQMLG VADLFNPQDP
WAHYITNALK AKELFVKDVN YIVRDGEAVI VDEFTGRVMP GRRWSDGQHQ AIEAKEALAI
QSETQTLASI TYQNFFLLYP RLAGMTGTAK TEEVEFEKTY KLETTIVPTN RVRARQDWAD
QVYKTEAAKW RAVANETAEI HKNGRPVLVG TTSVEKSELL SSLLAEQEIP HNLLNAKPEN
VERESEIVAQ AGRAGAVTIA TNMAGRGTDI ILGGNSDYMA RLKLREVLLG RLVKPEEDHT
PPVPLQRSAP GGFSDAAAPS LPRSGESLYP CPLTDDTDQA LGQLARDLVK AWGDRALTVI
ELEERIATAA EKAPTEAPQI QALREAIARV KGEYDAVVKQ EESRVREAGG LHVIGTERHE
SRRVDNQLRG RAGRQGDPGS TRFFLSLGDN LLRIFGGDRV AGLMNAFRVE EDMPIESGML
TRSLEGAQKK VETYYYDIRK QVFEYDEVMN NQRRAVYSER RRVLDGRALK KQVIGYGERT
MGEIVEAYVN PDLPPEEWDL DQLVGKVKEF IYLLEDLTPD QVQGLGMEEL KAFLQEQLRN
AYDLKEGQIE QQRPGLMREA ERFFILQQID TLWREHLQAM DALRESVGLR GYGQKDPLIE
YKNEGYDMFL EMMTNMRRNV IYSMFMFQPQ APKN
