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SECA_SYNY3
ID   SECA_SYNY3              Reviewed;         932 AA.
AC   Q55709; Q55065;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382};
DE            EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN   Name=secA {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=sll0616;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-777.
RX   PubMed=9988485; DOI=10.1046/j.1365-2958.1998.01145.x;
RA   Mazouni K., Bulteau S., Cassier-Chauvat C., Chauvat F.;
RT   "Promoter element spacing controls basal expression and light inducibility
RT   of the cyanobacterial secA gene.";
RL   Mol. Microbiol. 30:1113-1122(1998).
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:0000255|HAMAP-Rule:MF_01382}.
CC   -!- FUNCTION: Probably participates in protein translocation into and
CC       across both the cytoplasmic and thylakoid membranes in cyanobacterial
CC       cells. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01382}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01382}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}.
CC       Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01382};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01382};
CC       Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}. Cytoplasm
CC       {ECO:0000255|HAMAP-Rule:MF_01382}.
CC   -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01382}.
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DR   EMBL; BA000022; BAA10347.1; -; Genomic_DNA.
DR   EMBL; U38892; AAA96399.1; -; Genomic_DNA.
DR   PIR; S76501; S76501.
DR   AlphaFoldDB; Q55709; -.
DR   SMR; Q55709; -.
DR   IntAct; Q55709; 9.
DR   STRING; 1148.1001616; -.
DR   PaxDb; Q55709; -.
DR   EnsemblBacteria; BAA10347; BAA10347; BAA10347.
DR   KEGG; syn:sll0616; -.
DR   eggNOG; COG0653; Bacteria.
DR   InParanoid; Q55709; -.
DR   OMA; MVHYDVQ; -.
DR   PhylomeDB; Q55709; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015462; F:ABC-type protein transporter activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
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   GO; GO:0043952; P:protein transport by the Sec complex; IBA:GO_Central.
DR   CDD; cd18803; SF2_C_secA; 1.
DR   Gene3D; 3.40.50.300; -; 2.
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   PANTHER; PTHR30612; PTHR30612; 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; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF81767; SSF81767; 1.
DR   SUPFAM; SSF81886; SSF81886; 1.
DR   TIGRFAMs; TIGR00963; secA; 1.
DR   PROSITE; PS01312; SECA; 1.
DR   PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm; Membrane;
KW   Nucleotide-binding; Protein transport; Reference proteome; Thylakoid;
KW   Translocase; Translocation; Transport.
FT   CHAIN           1..932
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_0000109618"
FT   BINDING         90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         108..112
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         498
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   932 AA;  107009 MW;  B57502CDE3D69781 CRC64;
     MLKALFGDPN TRKLKKFQPY VAEVNLYEED IEKLSDDELK YKTVEFREAL DKARSDAETE
     EILDEILPEA FAVVREAGKR VLGMRHFDVQ LLGGIILHKG QIAEMKTGEG KTLVATLPSY
     LNGLTGKGVH VVTVNDYLAR RDAEWMGQIH RFLGLTVGLV QSGMNPEERK KNYACDITYT
     TNSELGFDYL RDNMSTAMIE VVQRPFNFCI IDEVDSILID EARTPLIISG QVERPTEKYL
     QASDIAAQLE PEIHYEVDEK QRNVLMTDEG FEKAEQLLQT TDLFDKNDPW AHYIFNAIKA
     KELFLKDVNY IVRNGEVVIV DEFTGRIMVG RRWSDGLHQA IEAKERVEIQ KESQTLATIT
     YQNFFLLYPK LSGMTGTAKT EETELEKVYN LQVTITPTNR PSSRQDWPDV VYKNEEAKWK
     AVALECEELH QQGRPILVGT TSVEKSEVIS RLLQSSGIHH NLLNARPENV ERESEIVAQA
     GRKGAVTIAT NMAGRGTDII LGGNSDYMAR LKVREYLMPK IVRPEDDELG AGVTGWVSGR
     EKPQGFGNQN GKKKVKTWQV SPDIYPTTIS QETEDLLKKA VKFAVDQYGL QSLTELEAED
     KLAIASEKGP TDDPVILKLR EVYNQIRREY EVLTSAEHKE VVELGGLHVI GTERHESRRV
     DNQLRGRAGR QGDPGSTRFF LSLEDNLLRI FGGDRVAGLM NMFRVEEDMP IESKMLTGSL
     EGAQKKVETY YYDIRKQVFE YDEVMNNQRK AIYAERRRVL EGLDLKEQVL VYAEKTMDEI
     VDAYVNPELP PEEWDVENML DKAKQFVYLL EDLTVEDLGD MTVWEMKTFF HEEVRKAYDL
     KETQVDKVRP GLMREAERYF ILQQIDNLWR EHLQSMEALR ESIGLRGYGQ KDPLIEYKQE
     GYEMFLEMMI DIRRNVVYSL FQFQPQQQPQ AV
 
 
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