ID A0A3A9KUV6_9BACI Unreviewed; 840 AA.
AC A0A3A9KUV6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 28-JAN-2026, entry version 27.
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=CR203_07870 {ECO:0000313|EMBL:RKL68386.1};
OS Salipaludibacillus neizhouensis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=885475 {ECO:0000313|EMBL:RKL68386.1, ECO:0000313|Proteomes:UP000281498};
RN [1] {ECO:0000313|EMBL:RKL68386.1, ECO:0000313|Proteomes:UP000281498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 13187 {ECO:0000313|EMBL:RKL68386.1,
RC ECO:0000313|Proteomes:UP000281498};
RA Wang H.;
RT "Bacillus sp. nov., a halophilic bacterium isolated from a Keqin Lake.";
RL Submitted (OCT-2017) 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:RKL68386.1}.
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DR EMBL; PDOE01000002; RKL68386.1; -; Genomic_DNA.
DR RefSeq; WP_110938726.1; NZ_KZ614147.1.
DR AlphaFoldDB; A0A3A9KUV6; -.
DR OrthoDB; 9805579at2; -.
DR Proteomes; UP000281498; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 1.10.3060.10:FF:000002; Preprotein translocase subunit SecA; 1.
DR FunFam; 3.40.50.300:FF:000429; Preprotein translocase subunit SecA; 1.
DR FunFam; 3.90.1440.10:FF:000001; 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; IPR004027; SEC_C_motif.
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; NF006630; PRK09200.1; 1.
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; 2.
DR Pfam; PF02810; SEC-C; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000281498};
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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 2..571
FT /note="SecA family profile"
FT /evidence="ECO:0000259|PROSITE:PS51196"
FT DOMAIN 88..248
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 415..570
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 786..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 104..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ SEQUENCE 840 AA; 96103 MW; 1AD8CF4A667485C1 CRC64;
MLGLLRKVIG DTDAKHIKKM QKTIDQIEAL SDDMKKLSDE ALRNKTTEFK ERYKNGEKLD
DLLPEAFAVV REGSTRSLGL THYQVQLVGG IVLHRGDISE MKTGEGKTLV ATLAVYLNAI
TEKGVHVVTV NEYLARRDAA EMGKLYTFLG LSVGLNLGGM TKEEKREAYK ADVTYGTNNE
LGFDYLRDNM VTYKEQMVQR PLYFAIVDEV DSILVDEART PLIISGSAQK TTELYTAANS
FVRMLKAEED YTYDEKAKNV QLADEGVSKA ERAFNIDNLF DSEHVQLNHN INQALKAHKV
MVRDEDYVVD DGEVAIVDQF TGRLMKGRRY SDGLHQAIEA KEGLEIKRES MTLASITFQN
YFRMYKKLAG MTGTAKTEEE EFRNIYAMNV YSIPTNEQIM REDRPDLIYK SAEGKFKAIV
EKIKELHEIG QPVLVGTVNV DTSELIANML KKKKVPHNVL NAKNHEREAE IIENAGQPKA
VTIATNMAGR GTDIKLGQGV TELGGLYVLG TERHESRRID NQLRGRAGRQ GDPGKSQFFI
SLEDTLMRRF ASDNMAKMME RLGMDEENPI ESKMITKAVE QAQKRVEGNN FDARKQLLQY
DDVMREQRDV IYEQRMEVLE SADLRPVVEK MLESTVERNV ALYTPESEVP EDWNLKGMVE
YINATVFSER EITEKDVHGL DSEEMIELIM EKVHEDYDDR EEAFTKDTMR EFERVILLRT
VDSKWTSHID QMDQLRQGIH LRAYGQNDPL REYKFEGFEM FEEMIATIEE EVSRYIMKAQ
IQSNLERKQV TEGKAVHEST AEKKETKRKT PFRKGETVKR NDPCPCGSGQ KYKNCHGQEQ
//
