SECA_PROMP
ID SECA_PROMP Reviewed; 943 AA.
AC Q7UZM1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=PMM1639;
OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS MED4).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1986 / NIES-2087 / MED4;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
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; BX548174; CAE20098.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7UZM1; -.
DR SMR; Q7UZM1; -.
DR STRING; 59919.PMM1639; -.
DR EnsemblBacteria; CAE20098; CAE20098; PMM1639.
DR KEGG; pmm:PMM1639; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_3; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000001026; 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_0000318413"
FT REGION 534..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..561
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; 107766 MW; 3541ED7AB70A933A CRC64;
MLKLLLGDPN TRKLKRYQPM VEEINLLEED VSILTDDELR NETHNLKSNI SSELNIKKQK
ELLEETLPKA FAIVREASKR VLEMRHFDVQ LIGGMVLHEG QIAEMKTGEG KTLVATLPCY
LNALTGKGVH VVTVNDYLAR RDAEWMGQVH RFLGLSVGLI QQDMSPAERK KNYACDITYA
TNSELGFDYL RDNMATEIEE VVQRKFNYCV IDEVDSILID EARTPLIISG QIERPQEKYQ
KAAELSLSLI KAKELSKDGI DPEGDYEVDE KQRSCILTDQ GFAKCEEALK VNDLYDPKDP
WAHYITNALK AKELFVKDVN YIIKKDEAVI VDEFTGRVMP GRRWSDGQHQ AIEAKEGLKI
QPETQTLASI TYQNFFLLYP GLAGMTGTAK TEEVEFEKTY KLESTVVPTN QIRKRQDWAD
QVFKTELGKW KAVANETAEI HRNGRPVLVG TTSVEKSELL SSLLFEQQIP HNLLNAKPEN
VEREAEIVAQ AGRSGAVTIA TNMAGRGTDI ILGGNSDYMA RLKLKETLMP LLVKPDNEHK
PPIPQQRNSK SGGGFSANVD SIANKNTKSG VDSLFPCQLG EDIKRKLSLL SNELVKNWGD
RSLTILELDD KIATAAEKAP TEDKLIQSLR ESLSEVKNEY EKVLIHEEEN VRNAGGLHVI
GTERHESRRV DNQLRGRAGR QGDLGSTRFF LSLEDNLLRI FGGDRVANLM NAFRVDEDMP
IESGMLTRSL ESAQKKVETY YYDIRKQVFE YDEVMNNQRK AVYNERLRVL KGNDLKKQVI
GYGERTMEEI VEAYINPDLP PEEWDIDQLI SKVKEFIYLL NDLKSEDVSV LSIEELKNYL
QEQLRIAYDL KEAQIEKFRP GLMREAERFF ILQQIDNLWR EHLQSMDSLR ESVGLRGYGQ
KDPLIEYKNE GYDMFLEMMT NMRRNVIYSM FMFQPKSEKV TNN
