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Database: UniProt
Entry: A0A3N5C0H5_9THEO
LinkDB: A0A3N5C0H5_9THEO
Original site: A0A3N5C0H5_9THEO 
ID   A0A3N5C0H5_9THEO        Unreviewed;       908 AA.
AC   A0A3N5C0H5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=EDD75_0481 {ECO:0000313|EMBL:RPF49661.1};
OS   Thermodesulfitimonas autotrophica.
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermodesulfitimonas.
OX   NCBI_TaxID=1894989 {ECO:0000313|EMBL:RPF49661.1, ECO:0000313|Proteomes:UP000282654};
RN   [1] {ECO:0000313|EMBL:RPF49661.1, ECO:0000313|Proteomes:UP000282654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 102936 {ECO:0000313|EMBL:RPF49661.1,
RC   ECO:0000313|Proteomes:UP000282654};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (NOV-2018) 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   -!- 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:RPF49661.1}.
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DR   EMBL; RKRE01000001; RPF49661.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N5C0H5; -.
DR   Proteomes; UP000282654; Unassembled WGS sequence.
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; SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM; 1.
DR   PANTHER; PTHR30612:SF0; SI:DKEY-187J14.7-RELATED; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   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}; Reference proteome {ECO:0000313|Proteomes:UP000282654};
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          19..645
FT                   /note="SecA family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51196"
FT   DOMAIN          105..263
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          863..897
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          20..47
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        863..885
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT   BINDING         121..125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT   BINDING         510
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   908 AA;  102540 MW;  69567AB088CC5CDF CRC64;
     MRNRDSTGSS FYAEGEETLI KILSNLLDDN AKEIKRLRRK VAEINALEPA VQALSDGDLA
     AKTAEFKNRL ARGESLDDLL PEAFAVVREA ARRVLGMRHF DVQLMGGIVL HQGRIAEMKT
     GEGKTLVATL PAYLNALTGK GVHIVTVNDY LARRDAEWMG SIYRFLGLSV GVIVHGLDWS
     ARKRAYNADV TYGTNNEFGF DYLRDNMALS PDEVVQRELN YAIVDEVDSI LIDEARTPLI
     ISGPSTKPTD LYYTFARLVP RLEAGKDYVV DEKAHTVSPT EAGVAKIEKW LKVDNLCDEK
     NIELMHHFRQ ALKAHALMKR DRDYVVKDGQ VIIVDEFTGR LMFGRRYSDG LHQAIEAKEG
     VKIERESQTL ATITFQNYFR MYKKLAGMTG TAATEEEEFR KIYGIDVVVI PTHKPMIRQD
     LPDMVFKTER AKFAAVVEEI ARRHATGQPV LVGTISIEKS ELISEMLKKR GIPHNVLNAK
     HHEKEAEIVA QAGRLGAVTI ATNMAGRGTD ILLGGNPVFM AKEEMRRRGY SPAVIAEAAE
     YGEPSSPEVA EARRVFREIL AAKTKITEAE REKVVALGGL HIIGTERHES RRIDNQLRGR
     CGRQGDPGST QFFCSLEDDL LRLFGGETIA NLATKLGVEE NVPIQHALVT RSLETAQKRV
     ENRNFSIRKQ VLEYDDVMNQ QREVIYGQRR QVLMEENLRE IITKMIEEVV ARTVATYCPE
     GVHQEEWDLN GLANYAAQVF LPDGIDPAEL AGKRRDEIKA LLLERAEAFY DAREKELGAP
     AMREIERWIL LRVVDEKWMD HLDAMEQLRE GIGLRAYGQR DPLIEYKFES YEMFQNMVAS
     IQEDAIRYLF RVRVAAAPER RQMVENRQSE DNGGRTVRRE QKVGRNDPCP CGSGKKYKKC
     CGRQVSAG
//
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