SECA_PROM2
ID SECA_PROM2 Reviewed; 943 AA.
AC A8G7E5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=P9215_19131;
OS Prochlorococcus marinus (strain MIT 9215).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=93060;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9215;
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; CP000825; ABV51526.1; -; Genomic_DNA.
DR RefSeq; WP_012008518.1; NC_009840.1.
DR AlphaFoldDB; A8G7E5; -.
DR SMR; A8G7E5; -.
DR STRING; 93060.P9215_19131; -.
DR EnsemblBacteria; ABV51526; ABV51526; P9215_19131.
DR KEGG; pmh:P9215_19131; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_3; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000002014; 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_0000318405"
FT REGION 535..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..564
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; 108211 MW; CE8740FFBCA338ED CRC64;
MLKLLFGDPN TRKLKRYQPI VEEINFLEEE ISQLTDDDLR KETQNLKSKI SSELDFKKQK
ELLEEFLPKA FAIVREASKR VLDMRHFDVQ LIGGMVLHEC QIAEMKTGEG KTLVATLPCY
LNALTGKGVH VVTVNDYLAR RDAEWMGQVH RFLGLSVGLI QQDMNPVERK KNYDCDITYA
TNSELGFDYL RDNMATDVNE VVQRKFNYCV IDEVDSILID EARTPLIISG QVERPQEKYQ
KAAQLSLKLV KAKELSKDGI DPEGDYEVDE KQRSCILTDQ GFAKCEEYLG VNDLYNPKDP
WAHYITNALK AKELFIKDVN YIIKNNEAVI VDEFTGRVMP GRRWSDGQHQ AIEAKESLQI
QPETQTLASI TYQNFFLLYP GLAGMTGTAK TEEVEFEKTY KLESTVIPTN QLRKRKDWSD
QVFKTEIGKW KAVAKETANI HRDGRPVLVG TTSVEKSELL SSLLSEEKIP HNLLNAKPEN
VEREAEIVAQ AGRAGAVTIA TNMAGRGTDI ILGGNSDYMA RLKLKEILIP LLVKPDNEHK
PPIPKQRNSK SKGGFSKKAS SKLKKNISNS STSLFPCKLD EAIEKQLSLL SDELVKNWGD
RQLSVLELDD RIATAAEKAP TDDDLIKLLR ESLSAVKKEY EKVLTHEEEK VRKAGGLHVI
GTERHESRRV DNQLRGRAGR QGDLGSTRFF LSLEDNLLRI FGGDRVANLM NAFRVDEDMP
IESGMLTRSL ESAQKKVETY YYDIRKQVFE YDEVMNNQRK AVYGERLRVL KGNDLKRQVI
GYGERTMSEI VDAYINPDLP PEEWNIDQLI SKVKEFIYLL DDLKSEDINL LSIEELKNYL
QEQLRIAYDL KESQIEKIRP GLMREAERFF ILQQIDNLWR EHLQSMDSLR ESVGLRGYGQ
KDPLIEYKNE GYDMFLEMMT NMRRNVIYSM FMFQPKTEVN EKK
