SECA_PROMA
ID SECA_PROMA Reviewed; 946 AA.
AC Q7V9M9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=Pro_1801;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(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; AE017126; AAQ00845.1; -; Genomic_DNA.
DR RefSeq; NP_876192.1; NC_005042.1.
DR RefSeq; WP_011125950.1; NC_005042.1.
DR AlphaFoldDB; Q7V9M9; -.
DR SMR; Q7V9M9; -.
DR STRING; 167539.Pro_1801; -.
DR EnsemblBacteria; AAQ00845; AAQ00845; Pro_1801.
DR GeneID; 54201130; -.
DR KEGG; pma:Pro_1801; -.
DR PATRIC; fig|167539.5.peg.1903; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_3; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000001420; 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..946
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000318403"
FT REGION 534..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 107..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 946 AA; 108056 MW; E9AF608123FCDCDA CRC64;
MLKLLLGDPN ARKLKRYQPI LTDINLFEDE IASLNDDELR GKTSDFRTRL DKSSDSSIQE
CLDDLLPEAF AVVREASKRV LGMRHFDVQL IGGMVLHEGQ IAEMKTGEGK TLVATLPSFL
NALTGRGVHI VTVNDYLARR DAEWMGQVHR FLGLSVGLIQ QDMTPIERRK NYECDITYAT
NSELGFDYLR DNMANDINEI VQRDFQFCII DEVDSILIDE ARTPLIISGQ IERPQEKYQK
AAEVVSTLQR AAEMGKDGID PEGDYEVDEK QRTCTLTDEG FAKSEELLKV KDLFDPKDPW
AHYITNALKA KELFVKDVNY IVRNEDAVIV DEFTGRVMPG RRWSDGQHQA IEAKEELPIQ
PETQTLASIT YQNFFLLYPR LAGMTGTAKT EEVEFEKTYK LETTVIPTNR PRSRADWVDQ
VFKTESAKWR AVANETVEIH KKGRPVLVGT TSVEKSEVLS ALLGEQDVPH NLLNAKPENV
EREAEIIAQA GRAGAVTIAT NMAGRGTDII LGGNSDYMAR LKVREVLFPK LVKPEDSHKP
PVPLQRRKDS SVGFGKEENN SKDKKVNHSN DVRAQENLYP CVLTDSTEQV LLDLEHQLIK
EWGDRVLSPI ELEDRISTAA EKAPTQDPLV QSLREAISLV KSEYDVVVKQ EEVHVREAGG
LHVIGTERHE SRRVDNQLRG RAGRQGDLGS TRFFLSLGDN LLRIFGGDRV AALMNAFRVD
EDMPIESGML TRSLESAQKK VETYYFDIRK QVFEYDEVMN NQRRAVYSER HRVLEGDELK
KQVIGYGERT MQEIVYAYVN PELPSEEWDL KQLVGKVKEF VYLLDDLKPK DIEALNIDEL
QAFLQEQLRN AYDLKESQIE ESRPGLMREA ERFFILQQID TLWREHLQSM DALRESVGLR
GYGQKDPLIE YKNEGYDMFL EMMTNMRRNV IYSMFMFQPA PPSDKE
