SECA_PROMM
ID SECA_PROMM Reviewed; 948 AA.
AC Q7V975;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=PMT_0083;
OS Prochlorococcus marinus (strain MIT 9313).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74547;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9313;
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; BX548175; CAE20258.1; -; Genomic_DNA.
DR RefSeq; WP_011129462.1; NC_005071.1.
DR AlphaFoldDB; Q7V975; -.
DR SMR; Q7V975; -.
DR STRING; 74547.PMT_0083; -.
DR EnsemblBacteria; CAE20258; CAE20258; PMT_0083.
DR KEGG; pmt:PMT_0083; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_3; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000001423; 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..948
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000318409"
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 948 AA; 107137 MW; ABD79A189DEEDEE0 CRC64;
MLKLLLGDPN ARKLKRYQPI VTDINILEED IALLSDDQLR SKTADFRQQF ENVVSFAKQR
ALLDELLPEA FAVVREAAKR VLGMRHFDVQ LIGGMVLHEG QIGEMKTGEG KTLVATLPSY
LNALTGRGVH VVTVNDYLAR RDAEWMGQVH RFLGLSVGLI QQDMSPAERR RNYACDITYA
TNSELGFDYL RDNMATDLSE VVQREFQYCV IDEVDSILID EARTPLIISG QVERPQEKYQ
QAADVAAALE RAAEQGKDGI DPEGDYEVDE KQRSCTLTDE GFAKAEQNLR VRDLFDPADP
WAHYITNALK AKELFVRDVN YIVRDGEAVI VDEFTGRVMP GRRWSDGQHQ AIEAKEQLAI
QPETQTLASI TYQNFFLLYP RLAGMTGTAK TEEVEFEKTY KLETSVIPTN QPRARADWVD
QVYKTESAKW RAVANETAEI HKQGRPVLVG TTSVEKSELL SSLLSEQEIP HNLLNAKPEN
VEREAEIVAQ AGRAGAVTIA TNMAGRGTDI ILGGNSDYMA RLKLREVLLP RLVRPEEGHR
PPVPLQRAAE TGGGFAAKAA ASNGSHGHVL SEARAIGSLY PCSLTDDTDQ FLAELARELV
KVWGDRALSV IELEDRISTA AEKAPTDDAQ IAALRESIAR VKTEYDVVVT QEEVRVREAG
GLHVIGTERH ESRRVDNQLR GRAGRQGDLG STRFFLSLED NLLRIFGGER VASLMNAFRV
EEDMPIESGM LTRSLEGAQK KVETYYYDIR KQVFEYDEVM NNQRRAVYAE RRRVLEGRGL
KKQVIGYGER TMDDIVEAYV NPDLPPEEWD LGQLVSKVQQ FVYLLEDLKP EQLQGLSMEE
LKSFLQEQLR NAYDIKEGQI EQQRPGLMRE AERFFILQQI DTLWREHLQA MDALRESVGL
RGYGQKDPLI EYKNEGYDMF LEMMANMRRN VIYSMFMFQP AASGQEQA
