ID A0A7X6D5L7_9ACTN Unreviewed; 926 AA.
AC A0A7X6D5L7;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 28-JAN-2026, entry version 20.
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 ECO:0000313|EMBL:NJQ08599.1};
GN ORFNames=HCN56_24245 {ECO:0000313|EMBL:NJQ08599.1};
OS Streptomyces lonarensis.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=700599 {ECO:0000313|EMBL:NJQ08599.1, ECO:0000313|Proteomes:UP000578686};
RN [1] {ECO:0000313|EMBL:NJQ08599.1, ECO:0000313|Proteomes:UP000578686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCL716 {ECO:0000313|EMBL:NJQ08599.1,
RC ECO:0000313|Proteomes:UP000578686};
RA Loughran R.M., Pfannmuller K.M., Wasson B.J., Deadmond M.C., Paddock B.E.,
RA Koyack M.J., Gallegos D.A., Mitchell E.A., Ushijima B., Saw J.H.,
RA Mcphail K.L., Videau P.;
RT "Draft genome of Streptomyces sp. ventii, isolated from the Axial Seamount
RT in the Pacific Ocean, and resequencing of the two type strains Streptomyces
RT lonarensis strain NCL 716 and Streptomyces bohaiensis strain 11A07.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00034006, 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NJQ08599.1}.
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DR EMBL; JAAVJD010000351; NJQ08599.1; -; Genomic_DNA.
DR RefSeq; WP_167974595.1; NZ_BHZG01000370.1.
DR AlphaFoldDB; A0A7X6D5L7; -.
DR Proteomes; UP000578686; Unassembled WGS sequence.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IEA:TreeGrafter.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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 GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-ARBA.
DR CDD; cd17928; DEXDc_SecA; 1.
DR CDD; cd18803; SF2_C_secA; 1.
DR FunFam; 1.10.3060.10:FF:000002; Preprotein translocase subunit SecA; 1.
DR FunFam; 3.40.50.300:FF:000113; Preprotein translocase subunit SecA; 1.
DR FunFam; 3.40.50.300:FF:000334; Protein translocase subunit SecA; 1.
DR FunFam; 3.90.1440.10:FF:000002; Protein translocase subunit 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-like.
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; NF009538; PRK12904.1; 1.
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:UP000578686};
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..245
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 871..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..926
FT /note="Basic 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 926 AA; 103657 MW; 7128B15187112A55 CRC64;
MSVFNKLMRA GEGKILRKLH RIANQVNSIE EDFLNLTDAE LRALTDEYRE RLAEGETLND
LMPEAFATVR EAAKRVLGQR HYDVQIMGGA AMHLGHVAEM KTGEGKTLVS TLPVYLNALA
GKGVHQITVN DYLAQRDSEW MGRVHKFLGL SVGCITGGMP PAKRREQYAC DVTHGTNNEF
GFDYLRDNMA WSKDELVQRG HFFAVVDEAD SILIDEARTP LIISGPADQA TKWYADFSKL
VKRLEKGEPA VPSRQVAETG DYDVDEKKRT VAIHDAGVAK VEDWLGIDNL YESVNTPLVG
YLNNAIKAKE LYKADKDYVV VDGEVVIVDE HTGRILAGRR YNEGMHQAIE AKEGVKIKDE
NQTLAKITLQ NYFRLYDTLS GMTGTAMTEA AELHQIYKLG VVPIPTHRGQ ARVDQADLIY
RTEVAKFAAV VEDVVEKHAT GQPVLVGTTS VEKSEYLSQQ LNKRGVRHEV LNAKNHEREA
SIVSKAGRRG AVTVATNMAG RGTDIKLGGN PDDIAETELR GKGLDPVEHL EEWAAALPEA
LERAERSVAT ENDAVKELGG LYVLGTERHE SRRIDNQLRG RSGRQGDPGE SRFYLSLGDD
LMRLFKAAMV ERVMSMANVP DDVPIENKMV TRAIASAQGQ VEQQNFEIRK NVLKYDEVLN
RQREVIYTER RRVLEGEDLH EQVRFFMDDT IDAYVQAETV EGFAEEWDLD RLWGAFKQLY
PIAVTVDELD DAVGDREGLT AEFIAESVKK DVYDQYDARE KELGSEVMRE LERRVVLSVL
DRKWREHLYE MDYLQEGIGL RAMAQRDPVV EFQREGFDMF TAMMEAIKEE SVGYLFNLEV
QVERKVEEVP VAEGAPAPRA AEAPAIKAKG LEAPQRTDRL HFSAPSVDGE GGVVEGDFDA
AGGSTTEGTG RAERRKAQKG GRRRKK
//
