ID F7QGI4_9BRAD Unreviewed; 942 AA.
AC F7QGI4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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:EGP09724.1};
GN ORFNames=CSIRO_0656 {ECO:0000313|EMBL:EGP09724.1};
OS Bradyrhizobiaceae bacterium SG-6C.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae.
OX NCBI_TaxID=709797 {ECO:0000313|EMBL:EGP09724.1, ECO:0000313|Proteomes:UP000003148};
RN [1] {ECO:0000313|EMBL:EGP09724.1, ECO:0000313|Proteomes:UP000003148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG-6C {ECO:0000313|EMBL:EGP09724.1,
RC ECO:0000313|Proteomes:UP000003148};
RX PubMed=21742875; DOI=10.1128/JB.05647-11;
RA Pearce S.L., Pandey R., Dorrian S.J., Russell R.J., Oakeshott J.G.,
RA Pandey G.;
RT "Genome Sequence of the Newly Isolated Chemolithoautotrophic
RT Bradyrhizobiaceae Strain SG-6C.";
RL J. Bacteriol. 193:5057-5057(2011).
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 both as a receptor for the
CC preprotein-SecB complex and as an ATP-driven molecular motor driving
CC the stepwise translocation of polypeptide chains across the membrane.
CC {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 -!- 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-YajC and YidC. {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:EGP09724.1}.
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DR EMBL; AFOF01000010; EGP09724.1; -; Genomic_DNA.
DR AlphaFoldDB; F7QGI4; -.
DR STRING; 709797.CSIRO_0656; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_5; -.
DR Proteomes; UP000003148; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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; 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}; Cytoplasm {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};
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 3..657
FT /note="SecA family profile"
FT /evidence="ECO:0000259|PROSITE:PS51196"
FT DOMAIN 89..247
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 900..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 105..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 525
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ SEQUENCE 942 AA; 106196 MW; 4FDF62FC16AAE237 CRC64;
MLGALARKFF GSANDRRIKG YQARVDAINK LEPEIAALSD EALKARTEEF RKQIAEGKSL
DDLLVPAFAT VREAAKRTLG QRHFDVQLIG GMVLHEGDIA EMKTGEGKTL VATLPVYLNA
LAGKGVHVVT VNDYLAKRDA GWMGQIYTFL GMSTGVIVHG LDDAERQAAY ACDITYGTNN
EYGFDYLRDN MKYRLEDMVQ RGHFFAIVDE VDSILIDEAR TPLIISGPLD DRSEFYNTID
TYIPKLEKVA DFEVDEKQRT VTLTEAGMEK IENLLQEAGQ LKGDSLYDVE NVSVVHHINQ
ALRAHSLFQR DKDYIVRDGE VVIIDEFTGR MMPGRRYSEG LHQALEAKEH QPVQPENQTL
ASITFQNYFR MYEKLAGMTG TAATEADELF DIYKLEVIEV PTNVPIARLD EDDEVYRTAD
EKHRAILDEI ERANKRMQPV LVGTASIEKS EVLGEYLQKN GYKQIDFGNP KALEKLYAAA
RAGKPAKLFA VLNARFHEQE AYIVAEAGVP GAITIATNMA GRGTDIKLGG SLEMRSQIET
EGVTDEAEKQ RIIDGIKADI EKFKEIVLKA EETVDLNPDK PGTKTIQKPG GLYIIGSERH
ESRRIDNQLR GRAGRQGDPG RTKFYLSLED DLMRIFGSDR LDTMLQRLGL KEGEAIIHPW
INKALEKAQQ KVEARNFDIR KNLLKFDDVQ NDQRKAIFDQ RIDLMRDQNV AETVSDMRHA
LVDDLVAKHI PEHAYAEQWD VAGLKEELKR VLDLDLPVDE WAKEEGIADE EMLARIEKRV
DEVMAAKSAQ FGPDVMRYVE KSILLQTLDH LWREHLVMLD HLRQVIGLRG YGQRDPLQEY
KSEAFNLFES LIAHLREAVT AQLVRVEIVP PDEQPELPQM EAHKLNPNTG EDEMAFAQAS
LAPVSPADRD PQNPATWGKV GRNEDCPCGS GKKFKHCHGK FA
//
