ID A0A0G3UKV7_9ACTN Unreviewed; 927 AA.
AC A0A0G3UKV7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Protein translocase subunit SecA {ECO:0000256|HAMAP-Rule:MF_01382, ECO:0000256|RuleBase:RU003874};
DE EC=7.4.2.8 {ECO:0000256|HAMAP-Rule:MF_01382};
GN Name=secA {ECO:0000256|HAMAP-Rule:MF_01382};
GN ORFNames=M444_14140 {ECO:0000313|EMBL:AKL66351.1};
OS Streptomyces sp. Mg1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=465541 {ECO:0000313|EMBL:AKL66351.1, ECO:0000313|Proteomes:UP000035653};
RN [1] {ECO:0000313|EMBL:AKL66351.1, ECO:0000313|Proteomes:UP000035653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mg1 {ECO:0000313|EMBL:AKL66351.1,
RC ECO:0000313|Proteomes:UP000035653};
RX PubMed=23908282;
RA Hoefler B.C., Konganti K., Straight P.D.;
RT "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT Single-Molecule Sequencing.";
RL Genome Announc. 1:e00535-13(2013).
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01382}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01382};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01382};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01382}. Cytoplasm
CC {ECO:0000256|HAMAP-Rule:MF_01382}. Note=Distribution is 50-50.
CC {ECO:0000256|HAMAP-Rule:MF_01382}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000256|ARBA:ARBA00007650,
CC ECO:0000256|HAMAP-Rule:MF_01382, ECO:0000256|RuleBase:RU003874}.
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DR EMBL; CP011664; AKL66351.1; -; Genomic_DNA.
DR RefSeq; WP_037797681.1; NZ_CP011664.1.
DR AlphaFoldDB; A0A0G3UKV7; -.
DR KEGG; strm:M444_14140; -.
DR PATRIC; fig|465541.12.peg.3062; -.
DR OrthoDB; 9805579at2; -.
DR Proteomes; UP000035653; 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: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; cd17928; DEXDc_SecA; 1.
DR CDD; cd18803; SF2_C_secA; 1.
DR Gene3D; 1.10.3060.10; Helical scaffold and wing domains of SecA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.90.1440.10; SecA, preprotein cross-linking domain; 1.
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 NCBIfam; TIGR00963; secA; 1.
DR PANTHER; PTHR30612:SF0; CHLOROPLAST PROTEIN-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR30612; SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM; 1.
DR Pfam; PF21090; P-loop_SecA; 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; SSF81886; Helical scaffold and wing domains of SecA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF81767; Pre-protein crosslinking domain of SecA; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01312; SECA; 1.
DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01382};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01382};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01382};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01382};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01382};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW Rule:MF_01382}; Reference proteome {ECO:0000313|Proteomes:UP000035653};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_01382};
KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW Rule:MF_01382};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01382}.
FT DOMAIN 1..626
FT /note="SecA family profile"
FT /evidence="ECO:0000259|PROSITE:PS51196"
FT DOMAIN 87..232
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 430..631
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 852..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..878
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 103..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 504
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ SEQUENCE 927 AA; 104284 MW; 33E4049F467D8E60 CRC64;
MSVFNKLMRA GEGKILRKLH RIADQVNSIE EDFVNLSDAE LRALTDEYKQ RYQDGESLDD
LLPEAFATVR EAAKRVLGQR HYDVQIMGGA ALHLGYVAEM KTGEGKTLVG TLPAYLNALS
GKGVHLITVN DYLAERDSEL MGRVHKFLGL EVGCILANMS PAQRREQYNS DITYGTNNEF
GFDYLRDNMA WSQDELVQRG HNFAVVDEVD SILVDEARTP LIISGPADQA TKWYADFAKL
VTRLTKGEPG QPLKGIEETG DYEVDEKKRT VAIHEAGVAK VEDWLGIENL YESVNTPLVG
YLNNAIKAKE LFKADKDYVV IDGEVMIVDE HTGRILAGRR YNEGMHQAIE AKEGVDIKDE
NQTLATITLQ NFFRLYSKLS GMTGTAMTEA AEFHQIYKLG VVPIPTNRDM VRKDQADLIY
RTEVAKFAAV VDDIAEKHEK GQPILVGTTS VEKSEYLSQQ LSKRGIPHEV LNAKQHEREA
SIVAQAGRRG AVTVATNMAG RGTDIKLGGN PDDLAEAELR QRGLDPEEHI EEWAQALPEA
LHRAEAAVKA EFEEVKDLGG LYVLGTERHE SRRIDNQLRG RSGRQGDPGE SRFYLSLGDD
LMRLFKAQMV ERVMSMANVP DDVPIENKMV TRAIASAQSQ VETQNFETRK NVLKYDEVLS
RQREVIYSER RRVLEGEDLQ EQVRHMMDDT IDAYIAAETV EGFAEEWDLD RLWGAFKQLY
PVKVTVEELE EAAGDRAGIT AEFIAESVKD DIHEQYEARE KTLGSEIMRE LERRVVLSVL
DRKWREHLYE MDYLQEGIGL RAMAQKDPLV EYQREGFDMF NAMQDGIKEE SVGYLFNLEV
QVEQQVEELP VQDAAPSLTK EPAGRPEIRA KGLDAPQRPD RLHFSAPTVD GEGGVVEGEF
DSEAGDGMTR AERRKAQKAA GGRRRKK
//
