SECA_BDEBA
ID SECA_BDEBA Reviewed; 889 AA.
AC Q6MR29;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=Bd0272;
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC Bdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
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-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; BX842646; CAE77929.1; -; Genomic_DNA.
DR RefSeq; WP_011162870.1; NC_005363.1.
DR AlphaFoldDB; Q6MR29; -.
DR SMR; Q6MR29; -.
DR STRING; 264462.Bd0272; -.
DR TCDB; 3.A.5.1.3; the general secretory pathway (sec) family.
DR PRIDE; Q6MR29; -.
DR EnsemblBacteria; CAE77929; CAE77929; Bd0272.
DR KEGG; bba:Bd0272; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_7; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000008080; 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; -; 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; 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; Translocase;
KW Translocation; Transport.
FT CHAIN 1..889
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000318324"
FT REGION 823..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..889
FT /note="Basic and acidic residues"
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 494
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 889 AA; 101164 MW; DDE3FF9A0DE42FB1 CRC64;
MVTQILTKMF GTKHDREMKK IQPTVDRINA LEPQMAALTD DQLKAKTPEF QERLKKGETV
HDILPEAFAV CREASKRVLG MRHYDVQLIG GYVLNRGNIA EMRTGEGKTL VATLPVYLNA
LTGRGVHVVT VNDYLVRRDA EHMGRLYGWL GLTTGIIVHG LTDQQRKQMY ACDITYCTNN
ELGFDYLRDN MKFDLNDYVQ RPHYYAIVDE CDSILVDEAR TPLIISGPAE SSTDKYYAVN
QIIPHLKRDV HFTMEEKSKT ASLTDAGNAK VEELMGLSNL YDPQNIEILH HVYQGLKAHY
LYRLDVEYMI KDGEIVIVDE FTGRLMPGRR WSDGLHQAIE AKEGVEVKSE NQTLATITFQ
NYFRMYEKLS GMTGTADTEA VEFKKIYNLE VNVIPTNRPI QRKDQEDVVY KSEKAKFKAI
TADIKERMAK GQPILVGTES IEKSEALSAF LRKEGVKHEV LNAKHHEREA EIIAQAGRKG
AVTIATNMAG RGTDIMLGGN ADMLAKAQVG NDDSPEFAEA VQKIKPQVEA ERAEVRSVGG
LYIIGTERHE SRRIDNQLRG RSGRQGDPGE SRFYLSLEDK LMRIFNGERI QKIMEMLNIP
EDEPITAKMV TNAIEGAQRK VEGHNFDIRK NLMEYDSVMN AQRNAIYGMR RKVLEGQEIE
RTTLDWLGDV VSNLLDTHIP EGGKKEEWSL EGLNNSLAQS FGFKIDFATM AVNTETVTDA
VKSGVKEVWE RQKNSMGPFF EQVQKMILLQ SIDHHWKNHL YVIDKLKEGI SLRGYAQKDP
LIEYKKEAFK AFETLNNTIK SDAIEKVMRV QLVAQQNEQE VLESLRPEEA DLDELDYSSP
SEADIGHSIP ETSEDAPKRK MTFQSGPRDD RPMNREERRR MDKDTKGKR
