ID A0A919T529_9ACTN Unreviewed; 763 AA.
AC A0A919T529;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=Protein translocase subunit SecA {ECO:0000256|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000256|HAMAP-Rule:MF_01382};
GN Name=secA_2 {ECO:0000313|EMBL:GIM85452.1};
GN Synonyms=secA {ECO:0000256|HAMAP-Rule:MF_01382};
GN ORFNames=Aco04nite_96340 {ECO:0000313|EMBL:GIM85452.1};
OS Winogradskya consettensis.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Winogradskya.
OX NCBI_TaxID=113560 {ECO:0000313|EMBL:GIM85452.1, ECO:0000313|Proteomes:UP000680865};
RN [1] {ECO:0000313|EMBL:GIM85452.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 14913 {ECO:0000313|EMBL:GIM85452.1};
RA Komaki H., Tamura T.;
RT "Whole genome shotgun sequence of Actinoplanes consettensis NBRC 14913.";
RL Submitted (MAR-2021) 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; 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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. 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}.
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:GIM85452.1}.
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DR EMBL; BOQP01000087; GIM85452.1; -; Genomic_DNA.
DR RefSeq; WP_213003864.1; NZ_BAAATW010000025.1.
DR AlphaFoldDB; A0A919T529; -.
DR Proteomes; UP000680865; 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:TreeGrafter.
DR CDD; cd17928; DEXDc_SecA; 1.
DR CDD; cd18803; SF2_C_secA; 1.
DR FunFam; 3.40.50.300:FF:000429; Preprotein 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; 3.
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; IPR026389; SecA_Actinobact-type.
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; TIGR04221; SecA2_Mycobac; 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:UP000680865};
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..574
FT /note="SecA family profile"
FT /evidence="ECO:0000259|PROSITE:PS51196"
FT DOMAIN 84..221
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 414..583
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 100..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ SEQUENCE 763 AA; 83805 MW; 46AE7F46301E3CAD CRC64;
MGVSQRLKSR FRKFLQRPGT TVDLGPLEKR LPAVEAREEA LQELDDEALT AAAGEAKTFE
EICAVGREAA RRALEQRPYD VQLLGAMALL SGKVAEMATG EGKTLTATVA AYGHVRLGNG
PVHVLTVNDY LARRDATWME PVYKLLGLTV GWVTEASTPQ ERREAYAADV TYVSVSEAGF
DYLRDQLVTD VEDRVQRALA TAIVDEADSI LIDEARVPMV LAGNVVGESD PVHNAADLVR
ALRPGKDFEV ADDGRSVAFT DAGLKALEEK MDLDLYSDEH VAELSAVNVA LHAEALLRRD
VDYIVRDGSV ELIDEMRGRV AQRRRWPDGL QAAVEAKEGL RATAEGEVLD TITVQAYIAL
YKTVCGMTAT AVHVGEQLRE YFKLEVAVIP SNTPNIREDE PDRIYSAHDM RDEALVEEIK
IAHEKGRPVL IGTLDVKASE LLAKQLAAAG VPSVVLNAKN DDEEATIIAE AGALGAVTVS
TQMAGRGVDI RLGGSDEKDR DAVVELGGLF VIGSGRHDSR RVDDQLRGRA GRQGDPGGSV
FFVSLEDNLV TRHAGDILPS SPRMDMDGVV HDDQVDYAVE HAQRVAEGVN HEIHRNTWRY
SVVIEQQRIA LAERRERLLT SEVATIMLLE RSPEKAKETD EDVLSDAARA IALYHLDRLW
VDHLAELSEV REGVHLRALG KLDPLDEFHR AAVPAFQKVF TEIESRTIAT FEEVDLTDGW
EPDRADLVRP SATWTYLVHD NPFGSELDRL IAAVGRRLTS GAE
//
