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Database: UniProt
Entry: A0A238U938_9FLAO
LinkDB: A0A238U938_9FLAO
Original site: A0A238U938_9FLAO 
ID   A0A238U938_9FLAO        Unreviewed;      1116 AA.
AC   A0A238U938;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
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:SNR15516.1};
GN   ORFNames=TJEJU_1807 {ECO:0000313|EMBL:SNR15516.1};
OS   Tenacibaculum jejuense.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=584609 {ECO:0000313|EMBL:SNR15516.1, ECO:0000313|Proteomes:UP000215214};
RN   [1] {ECO:0000313|EMBL:SNR15516.1, ECO:0000313|Proteomes:UP000215214}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=type strain: KCTC 22618 {ECO:0000313|Proteomes:UP000215214};
RA   Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL   Submitted (JUL-2017) 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}.
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DR   EMBL; LT899436; SNR15516.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238U938; -.
DR   KEGG; tje:TJEJU_1807; -.
DR   OrthoDB; 9805579at2; -.
DR   Proteomes; UP000215214; Chromosome tjeju.
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; 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   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; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000215214};
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..770
FT                   /note="SecA family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51196"
FT   DOMAIN          178..337
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          618..786
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1025..1074
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          53..80
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1025..1044
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1045..1070
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT   BINDING         194..198
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT   BINDING         692
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   1116 AA;  127817 MW;  4FB654EC3DF80213 CRC64;
     MSILNSIIKI FVGDKQQKDL KKLQPIIDNI KAFNDDLAKL SHDELRAKTV EFKSKITAAT
     QSFEDQISQL EEEVKSADID RQEDIYTQID KLKDEAYEAS EQVLKDIMSE AFAVVKETAR
     RFATNENIEV NATPFDRELS ATREHIELDG DKALWANTWD ASGKEVTWDM IHYDVQLIGG
     SVLHNGKIAE MMTGEGKTLV STLPVYLNAL TGKGVHVVTV NDYLAKRDRA WMAPIFEFHG
     LSTDCIDFHQ PNSEERRKAY NADITYGTNN EFGFDYLRDN MASSKEDLVQ RAPNYAIIDE
     VDSVLIDDAR TPLIISGPIP QGDIHEFNEL KPLVADLVSL QSKYLVGVLS EAKKLLKEGD
     TKEGGFLLLR VYRGLPKNKA LIKFLSQEGI RQILQKTENF YMQDNNKLMP EVDAELWFTI
     EEKNNQINLT DKGVGHLSER TQNDTFFVLP DISIKIAEID GNEGTPEQKA ELKEELYRDF
     SVKSERIHTM NQLLKAYTLF EKDVEYVVVD NKVMIVDEQT GRIMDGRRYS DGLHQAIEAK
     ESVKIEDATQ TFATVTLQNY FRMYRKLSGM TGTAVTEAGE FWEIYKLDVV EIPTNKPIAR
     DDKEDLLYKT TREKYNAVIE EIVKLVGENR PVLVGTTSVE ISELLGRMLK MRKIPHNILN
     AKLHKKEADI VAEAGKPGQV TIATNMAGRG TDIKLSDEVK AAGGLAIIGT ERHDSRRVDR
     QLRGRAGRQG DVGSSQFFVA LDDNLMRLFG SDRIAKVMDR LGLKEGEVIQ DRMVTRSIER
     AQKKVEENNF GIRKRLLEYD DVMNAQREFV YKRRRHALDG KRLQIDIANM IYDTCDAVVR
     QNKLTKDFQN FEFELIRFSS MTSPFTEDEF NAKPEQELID QLYKLVTENY KADADRNASQ
     VYPVIKGVFE NEGDRYERIV VPFTDGTKTL RVVTNLKEAY ESKGKSLVND FEKNITLAII
     DENWKDHLRK MDELKQTVQN ATYEQKDPLL VYKFEAFELF QKTIDKVNKE VLSFLFKGKL
     PQEDESQISE AQEQKREQLD LRKDEVQNST QQAISNARQQ QTQEQQAVET VVREQPKIGR
     NERVTIKNVM SGEEKEVKYK QAIPLLEQGT WVLYNK
//
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