SECA_PSEAE
ID SECA_PSEAE Reviewed; 916 AA.
AC Q9LCT3; Q7DC74;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=PA4403;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RA Levesque R.C., Liao X., Lightfoot J., Charlebois I., Ouellet C.,
RA Morency M., Dewar K., Siehnel R., Lam J., Hancock R.E.;
RT "Physical mapping of 38 loci including aimE, ampC, ampR, arcA, aroK, catR,
RT cypH, dapB, envA, envC, ftsA, ftsZ, groEL, murE, opdE, oprD, oprF, oprH,
RT oprI, oprK, oprP, pbpB, pbpC, pheS, phoA, phoB, phoS, ponA, pyoS1, qin,
RT rpoB, rpoH, sodB, soxR, sucC.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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 both as a receptor for the
CC preprotein-SecB complex and as an ATP-driven molecular motor driving
CC the stepwise translocation of polypeptide chains across the membrane.
CC {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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01382};
CC Note=May bind 1 zinc ion per subunit. {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-YajC and YidC. {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 Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-
CC 50. {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; U19797; AAF26459.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07791.1; -; Genomic_DNA.
DR PIR; D83093; D83093.
DR RefSeq; NP_253093.1; NC_002516.2.
DR RefSeq; WP_003112752.1; NZ_QZGE01000004.1.
DR AlphaFoldDB; Q9LCT3; -.
DR SMR; Q9LCT3; -.
DR STRING; 287.DR97_1581; -.
DR PaxDb; Q9LCT3; -.
DR PRIDE; Q9LCT3; -.
DR EnsemblBacteria; AAG07791; AAG07791; PA4403.
DR GeneID; 881307; -.
DR KEGG; pae:PA4403; -.
DR PATRIC; fig|208964.12.peg.4611; -.
DR PseudoCAP; PA4403; -.
DR HOGENOM; CLU_005314_3_0_6; -.
DR InParanoid; Q9LCT3; -.
DR OMA; MVHYDVQ; -.
DR PhylomeDB; Q9LCT3; -.
DR BioCyc; PAER208964:G1FZ6-4489-MON; -.
DR BRENDA; 7.4.2.5; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015462; F:ABC-type protein transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 GO; GO:0043952; P:protein transport by the Sec complex; IBA:GO_Central.
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; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004027; SEC_C_motif.
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; PF02810; SEC-C; 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 Metal-binding; Nucleotide-binding; Protein transport; Reference proteome;
KW Translocase; Translocation; Transport; Zinc.
FT CHAIN 1..916
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000287812"
FT REGION 857..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 105..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 900
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 902
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 911
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 912
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 916 AA; 103855 MW; D2B2FE82D07F651F CRC64;
MFAPLLKKLF GSKNERDVKR MAKAVQAINA LEPQMVALSD EQLKAKTAEF QQRYAKGETL
DQLLPEAFAV VREAGKRVMG MRHFDVQLIG GMTLHDGKIA EMRTGEGKTL VGTLPVYLNA
LSGKGVHVVT VNDYLARRDA NWMRPLYEFL GLSVGVVTPF QPPEDKRAAY AADITYGTNN
EFGFDYLRDN MAFSLDDKFQ RELNFAVVDE VDSILIDEAR TPLIISGQAE DSSELYIKIN
KLIPRLKRQV EEVEGKPTEE GHYSIDEKTR QVELNEQGHQ FIEDLLSQNG LLGEGESLYS
AHNLSLLTHV YAALRAHTLF HRNVEYIVQG DQILLIDEHT GRTMPGRRLS EGLHQAIEAK
EGLPIQAESQ TLASTTFQNY FRLYNKLAGM TGTADTEAFE FRQIYGLDVV VIPTHRPIAR
KDFNDLVYLT QEEKYAAIIT DIKQCQALGR PILVGTASIE SSEYVSKLLQ EAGIEHKVLN
AKYHEKEAEI IAQAGAPGSV TIATNMAGRG TDILLGGNWE VEVAALENPT EEQIAQIKAE
WQKRHQQVIE AGGLHVIASE RHESRRIDNQ LRGRAGRQGD PGSSRFYLSL EDNLMRIFAS
DRVKNFMKAL GMQSGEAIEH RMVTNAIEKA QRKVEGRNFD IRKQLLEFDD VANEQRKVIY
HMRNTLLSAE DVGETIKEFR EETLSATINQ HIPPQSLPEQ WDIEGLEAAL YSDFAVRLPI
QQWLDEDDKL YEETLRSKIL EQIVAAYYEK EELAGAEALR AFEKQMLLRV LDDLWKDHLS
TMDHLRHGIH LRGYAQKNPK QEYKRESFTL FQELLDSIKR DTIRVLSHVQ VRREDPAEEE
ARLRREAEEL AKRMQFQHAE APSMEQAVAG EEEELPEGPA PVVPLEPVRN EQKIGRNEPC
PCGSGKKYKH CHGQLD
