SECA_FLAPJ
ID SECA_FLAPJ Reviewed; 1116 AA.
AC A6GX63;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=FP0581;
OS Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS JIP02/86).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=402612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86;
RX PubMed=17592475; DOI=10.1038/nbt1313;
RA Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B.,
RA Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F.,
RA Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT psychrophilum.";
RL Nat. Biotechnol. 25:763-769(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 -!- 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 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM398681; CAL42686.1; -; Genomic_DNA.
DR RefSeq; WP_011962742.1; NC_009613.3.
DR RefSeq; YP_001295502.1; NC_009613.3.
DR AlphaFoldDB; A6GX63; -.
DR SMR; A6GX63; -.
DR STRING; 402612.FP0581; -.
DR EnsemblBacteria; CAL42686; CAL42686; FP0581.
DR GeneID; 66552739; -.
DR KEGG; fps:FP0581; -.
DR PATRIC; fig|402612.5.peg.593; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_10; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000006394; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma 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; -; 3.
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; 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; SM00490; HELICc; 1.
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 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; Translocase;
KW Translocation; Transport.
FT CHAIN 1..1116
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000320812"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 195..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 692
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 1116 AA; 127175 MW; 06918C20AF416A96 CRC64;
MSFINNILKV FVGDKSQKDV KAIQPIIAKI RTLENSLSNL SHDELRAKTV YFKDIIKQAR
AEKDTKIENL KLEVEAIQDI DAREDVYAQI DILEKEAYEI SEKTLNEILP EAFAVIKETA
KRFKENKQIT VTATAKDREL SATKSYINLV GDTAVWANSW SAAGKEITWD MIHYDVQLIG
GVVLHQGKIS EMQTGEGKTL VATLPLYLNA LTGNGVHLVT VNDYLAKRDS AWKAPLFEFH
GLMVDCIDLH QPNSDARRKA YDADITYGTN NEFGFDYLRD NMAHSPEDLV QRKHNFAIVD
EVDSVLIDDA RTPLIISGQV VDGDRHEFTE LKPKIENLVN IQRQLANGFL TEAKRLIKEG
NTKDGGFQLL RAHRALPKNK ALIKFLSEEG IKALLQKTEN QYMSDNNREM PKVDEALYFV
IEEKNNQVEL TDSGIEIMSK DTEDTFFVLP DIGTEIARIE KLNLSTEEQG EQKEKLFQDF
SVKSERIHTL TQLLKAYTLF EKDTEYVLMD NKVMIVDEQT GRIMDGRRYS DGLHQAIEAK
ENVKIEDATQ TYATVTLQNY FRMYSKLAGM TGTAVTEAGE LWEIYKLDVV EIPTNRGMSR
IDKEDLIYRS VREKFNAVIE DVVGLSQSGR PVLIGTTSVE ISELLSRMLK MRNIPHNVLN
AKMHKQEAQI VEEAGKPGVV TIATNMAGRG TDIKLTAEVK AAGGLAIIGT ERHDSRRVDR
QLRGRAGRQG DPGSSQFYVS LEDNLMRLFG SDRVAKIMDR MGLQEGEVIQ HSMMTKSIER
AQKKVEENNF GTRKRLLEYD DVMNSQREVV YKRRRHALHG ERLKLDIANM MYDTCEVIVE
KNKLTGDFKN FEFELIKNLS ITSPVTQADF AKLSDIELTG KTYKAASEYY TEKNIRDAHE
AFPIIRNVYE NPGNSFERII VPFTDGIKSL NVVTDLKKAY ESQGKQLVAD FEKNITLAIV
DDAWKKHLRK MDEMKQSVQL AVHEQKDPLL IYKFEAFKLF KNMLDGINKE VISFLFKGDL
PQQQNNIQEA TQIRQKENYI ESKDEILNIE EQAERNHEAG QTQQHQVTET IVRDMPKINR
NDTVKIQNVA NGQIEELKFK KAEILLNAGT WVLVSE
