GenomeNet

Database: UniProt
Entry: A0A0F7JK54_9DEIO
LinkDB: A0A0F7JK54_9DEIO
Original site: A0A0F7JK54_9DEIO 
ID   A0A0F7JK54_9DEIO        Unreviewed;       869 AA.
AC   A0A0F7JK54;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=SY84_02335 {ECO:0000313|EMBL:AKH16072.1};
OS   Deinococcus soli (ex Cha et al. 2016).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=1309411 {ECO:0000313|EMBL:AKH16072.1, ECO:0000313|Proteomes:UP000034024};
RN   [1] {ECO:0000313|EMBL:AKH16072.1, ECO:0000313|Proteomes:UP000034024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N5 {ECO:0000313|EMBL:AKH16072.1,
RC   ECO:0000313|Proteomes:UP000034024};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Deinococcus soli/N5/whole genome sequencing.";
RL   Submitted (JAN-2015) 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, ECO:0000256|RuleBase:RU003874}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP011389; AKH16072.1; -; Genomic_DNA.
DR   RefSeq; WP_046842647.1; NZ_CP011389.1.
DR   AlphaFoldDB; A0A0F7JK54; -.
DR   KEGG; dch:SY84_02335; -.
DR   PATRIC; fig|1309411.5.peg.490; -.
DR   OrthoDB; 9805579at2; -.
DR   Proteomes; UP000034024; 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: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; 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; 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   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:UP000034024};
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          2..653
FT                   /note="SecA family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51196"
FT   DOMAIN          87..248
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
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         508
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   869 AA;  97229 MW;  EEF2A4CEA1F9FF13 CRC64;
     MFRVLNKMFD NNQRDVAQII KTIVQPVNAL EEETQKVEDL AAAFMELRRR VTEGGETLDD
     VVVPAFALIR EAGRRSIGKR HYDVQLIGGY ALHKGRIAEM RTGEGKTLVA TLALALNALE
     GRGCHLVTVN DYLARVGMEE MSLLYRTLGL TVGLASREMQ PHQKQAAYAC DITYVTNSEL
     GFDYLRDNMA QSREALALRA EHPLNFAIVD EVDSILIDEA RTPLIISGAA EKATDLYYVY
     AKLIRRLQKG EPAEPGVRAE PTGDYTIDEK GKQVHITEGG ISKIERLLSL SDLYSPDNMD
     KAHMITQAIR ARELYHREKD YIVNAEGEVI IIDEFTGRSM PGRRYGEGLH QAIEAKEGVK
     IENENQTLAT ITYQNFFRLY NKFAGMTGTA KTEEKEFLDI YGSDVLVIPT NRGVQRKDAE
     DLVYRTKMGK YNAVVQEVKE MHATGRPVLI GTASIVTSEQ LSDLLTQAGI QHSVLNAKFE
     AQEASIVAQA GRSGTVTIAT NMAGRGTDIM LGGNAEFILG EAIEQQLGLS RYTPEVENFI
     KAISRQDPDA MQIGMQIPGM NEDFIGQAIQ LQADTLADRQ RVKDLGGLHI IGTERHESRR
     IDNQLRGRAG RQGDPGSSRF YVSFEDDLMR LFANDRVVAM MDRLGMDDTQ PIEAKMVTGA
     IEKAQARVED RNFSTRKQLL EFDNVMSKQR DTVYAQRREV LLGPDADVEE STEGMIADFV
     DHQLATHLPI DQNHESWDID GLRAAITDAV PQLEEFDFES LRSKSPAEAQ DTLLAAVADA
     FDARKEELSP TMMNSLSRYV VLQVVDQLWK EHLHGMDVLR QGIGLRGYGQ RDPFTEYKFE
     ATTMFNDMID TLKADVTKFV FRMQFGQAG
//
DBGET integrated database retrieval system