ID A0A9X4H048_9FIRM Unreviewed; 886 AA.
AC A0A9X4H048;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 10.
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:MDF9406981.1};
GN ORFNames=L7E55_01160 {ECO:0000313|EMBL:MDF9406981.1};
OS Pelotomaculum isophthalicicum JI.
OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
OC Desulfotomaculaceae; Pelotomaculum.
OX NCBI_TaxID=947010 {ECO:0000313|EMBL:MDF9406981.1, ECO:0000313|Proteomes:UP001154312};
RN [1] {ECO:0000313|EMBL:MDF9406981.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JI {ECO:0000313|EMBL:MDF9406981.1};
RA Leng L.;
RL Submitted (FEB-2022) 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:MDF9406981.1}.
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DR EMBL; JAKOAV010000001; MDF9406981.1; -; Genomic_DNA.
DR RefSeq; WP_277442126.1; NZ_JAKOAV010000001.1.
DR AlphaFoldDB; A0A9X4H048; -.
DR Proteomes; UP001154312; Unassembled WGS sequence.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IEA:UniProtKB-ARBA.
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: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; 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; 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; 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; 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:UP001154312};
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 1..621
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 REGION 845..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..862
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 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ SEQUENCE 886 AA; 101381 MW; 3F3F438D639946B9 CRC64;
MLGFIKDWLD DNAREVKKLQ QVVNKINSLE PKMSAMPEEE LKNMTVVFRE RLEQGQTLDD
ILPEAFAVVR EVSRRVLGMR HFDVQLLGGI VLHQGRIAEM KTGEGKTLVA TLPVYLNALT
GKGVHVITVN DYLARRDSEW MGQIYSYLGL NVGLVLHGLE WEDRRRAYRS DITYGTNNEF
GFDYLRDNMA QHPDQLVQRE LNYAIVDEVD SILIDEARTP LIISGQAEKS TDLYFTFAKV
VPRLIRETDY NVDEKAHTVA ITESGVAKVE KMISVENLYD DKNIELAHHL NQALKAYGLM
KRDRDYVVKD GQVIIVDEFT GRLMFGRRYS DGLHQAIEAK EGVKIERESQ TLATITFQNY
FRMYDKLAGM TGTAATEEQE FKKIYDLDVV VIPSNKPMIR KDLPDVIYKT EQAKFSAVVE
EIAARHDKRQ PVLVGTISIE KSEILSNMLR RRGIAHQVLN AKYHDKEAEI VAQAGRAGAV
TIATNMAGRG TDILLGGNPE FLTRYELRKQ GHEFEAAGEI TSVAAGADDT VYRALLEKYR
AQSEEERRLV VEQGGLHIMG TERHESRRID NQLRGRCGRQ GDPGSTQFYS SLEDDLLRLF
GSENISGIMD RLGIEEDMPI EHGMITRSIE TAQKRVENRN FDIRKHVLQY DDVMNQQREL
IYRQRRQVLT GGNLKENIME MIGAAVERAV ATYAPEGVYP EEWDLKGLLE YSEQIFLPNS
GLSPEDLEGM GRNELQSFLV ERSSEMYEAR EQELGGEMMR EIERVVMLRI VDEKWMDHLD
AMDQLREGIG LRAYGQKDPL VEYKFEGYEM FQNMIDSIQD DVVRYIFRVN VVQPEQRQKR
QVIENRYAEE GPKQPVRREN KVGRNSPCPC GSGKKYKKCC GRAEAV
//
