SECA_PROM5
ID SECA_PROM5 Reviewed; 943 AA.
AC A2BZ24;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=P9515_18281;
OS Prochlorococcus marinus (strain MIT 9515).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167542;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9515;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(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; CP000552; ABM73035.1; -; Genomic_DNA.
DR AlphaFoldDB; A2BZ24; -.
DR SMR; A2BZ24; -.
DR STRING; 167542.P9515_18281; -.
DR EnsemblBacteria; ABM73035; ABM73035; P9515_18281.
DR KEGG; pmc:P9515_18281; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_3; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000001589; 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..943
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000318410"
FT REGION 534..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..576
FT /note="Polar residues"
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 943 AA; 107626 MW; 47F206A1997954C3 CRC64;
MLKLLLGDPN TRKLKRYQPI VEEINLLEEE VSILTDDELR NETHNLKSKV SLEINIKRQN
EKLEEILPKA FAIVREASKR VLEMRHFDVQ LIGGMVLHEG QIAEMKTGEG KTLVATLPCY
LNALTGKGVH VVTVNDYLAR RDAEWMGQVH RFLGLSVGLI QQDMSPAERK KNYACDITYA
TNSELGFDYL RDNMATEIEE VVQRKFNYCV IDEVDSILID EARTPLIISG QIERPQEKYQ
KAAELALSLI KAKELSKDGI DPEGDYEVDE KQRSCILTDQ GFAKCEESLK VNDLYDPQDP
WAHYITNALK AKELFVKDVN YIIKKDEAVI VDEFTGRVMP GRRWSDGQHQ AIEAKEGLKI
QPETQTLASI TYQNFFLLYP GLAGMTGTAK TEEVEFEKTY KLESTVVPTN QVRKRQDWAD
QVFKTEIGKW KAVANETAEI HRNGRPVLVG TTSVEKSELL SSLLFEQQIP HNLLNAKPEN
VEREAEIVAQ AGRSGAVTIA TNMAGRGTDI ILGGNSDYMA RLKLKETLMP LLVKPDNEHK
PPIPQQRSSK AGGGFASKSE SISNKNSKSS GASLFPCQLG EDTTRKLSLL SNELVKSWGE
RTLTILELDD RIATAAEKAP TEDKLIQSLR DALSDVKNEY EKVLVHEEEN VRKAGGLHVI
GTERHESRRV DNQLRGRAGR QGDLGSTRFF LSLEDNLLRI FGGDRVANLM NAFRVDEDMP
IESGMLTRSL ESAQKKVETY YYDIRKQVFE YDEVMNNQRK AVYNERLRVL KGSDLKKQVL
GYGDRTMEEI VEAYINPDLP PEEWDIEQLI SKVKEFIYLL NNLKSTDVSV LSVEELKNYL
QEQLRIAYDL KEAQIEQFRP GLMREAERFF ILQQIDNLWR EHLQSMDSLR ESVGLRGYGQ
KDPLIEYKNE GYDMFLEMMT NMRRNVIYSM FMFQPQSEKE TKS
