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Database: UniProt
Entry: A0A494Y281_9BACL
LinkDB: A0A494Y281_9BACL
Original site: A0A494Y281_9BACL 
ID   A0A494Y281_9BACL        Unreviewed;       743 AA.
AC   A0A494Y281;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
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 {ECO:0000256|HAMAP-Rule:MF_01382};
GN   ORFNames=D7Z26_02375 {ECO:0000313|EMBL:RKP56856.1};
OS   Cohnella endophytica.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=2419778 {ECO:0000313|EMBL:RKP56856.1, ECO:0000313|Proteomes:UP000282076};
RN   [1] {ECO:0000313|EMBL:RKP56856.1, ECO:0000313|Proteomes:UP000282076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M2MS4P-1 {ECO:0000313|EMBL:RKP56856.1,
RC   ECO:0000313|Proteomes:UP000282076};
RA   Tuo L.;
RT   "Cohnella sp. M2MS4P-1, whole genome shotgun sequence.";
RL   Submitted (OCT-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   -!- 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}.
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:RKP56856.1}.
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DR   EMBL; RBZM01000002; RKP56856.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A494Y281; -.
DR   OrthoDB; 9805579at2; -.
DR   Proteomes; UP000282076; 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: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; 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.
DR   InterPro; IPR027417; P-loop_NTPase.
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   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; PF07517; SecA_DEAD; 1.
DR   Pfam; PF01043; SecA_PP_bind; 1.
DR   Pfam; PF07516; SecA_SW; 2.
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:UP000282076};
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          5..579
FT                   /note="SecA family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51196"
FT   DOMAIN          89..286
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          416..585
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
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         494
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   743 AA;  83445 MW;  D7E957C6D8D2635D CRC64;
     MNFASKLVQK VKDRFVQHKL KPYADKLKEI QLLRLETWDD GKLKAESLKL KKQVQDGTSL
     DDILIEAFAI AGEAASRVLG MRPFDVQYMA GLVLHEGNLV EMQTGEGKTL AAVMPAYVNA
     LQGKGVHVLT FNDYLAGRDA EWMGPIYQYL GLSVGFVKEG MTLEERQQAY SADITYVTAK
     QAGFDYLRDT IAMNPTDVVH RPFHYAIVDE ADSLLIDEAR VPLVIAGEVA STGGDGGRMA
     NLARQLVLGE DYDFDENKRN VFLTEAGAEK AEQALRSGNL YESNNTHLLT SLNCALHAES
     LLKRDVDYVI RDGKLELIDP YTGRVAENRH WPDGLQAAVE AKEGMASNTS GKILGTITLQ
     HLLSLYPKIS GMTATAQDSA EEFEETYNLL VFEIQPNRPR IRIDHESRIF THKEARLNAL
     VKEIAEVHAT KRPILIGTSS VEESDQLAER LKAAGVTCHV LNAKNDEKEA EIIANAGELG
     AVTVSTNMAG RGVDIRLGGG HPEQADQVAK LGGLYVIGTH MNESARIDNQ LRGRAGRQGD
     PGSSRFYVCL EDELINRFGI EKALPPAYRN KKQDEPLEAS IFNKKIDHIQ RIVMGQNFEM
     RKTLNKYSDM VEEQRRIQQE QREAIFDNRE SLSSTERYVR LYHMDRSWSD HLAYVSYIRE
     GIHLESLANR NPVDEFHHRI IHAFEQLPEK IDKETAKTLS KLKTGTPSDQ VDWDKEGLKA
     PSKTWTYLIQ DQFMEKKSNI FGL
//
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