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SECA_CHLT2
ID   SECA_CHLT2              Reviewed;         969 AA.
AC   B0B8S7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=CTL0070;
OS   Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=471472;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=434/Bu / ATCC VR-902B;
RX   PubMed=18032721; DOI=10.1101/gr.7020108;
RA   Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA   Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA   Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT   "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT   venereum isolates.";
RL   Genome Res. 18:161-171(2008).
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   -!- 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       Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-
CC       50. {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; AM884176; CAP03514.1; -; Genomic_DNA.
DR   RefSeq; WP_009873306.1; NC_010287.1.
DR   RefSeq; YP_001654161.1; NC_010287.1.
DR   AlphaFoldDB; B0B8S7; -.
DR   SMR; B0B8S7; -.
DR   EnsemblBacteria; CAP03514; CAP03514; CTL0070.
DR   KEGG; ctb:CTL0070; -.
DR   PATRIC; fig|471472.4.peg.75; -.
DR   HOGENOM; CLU_005314_0_0_0; -.
DR   OMA; MVHYDVQ; -.
DR   Proteomes; UP000000795; 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: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   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; 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; 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; Translocase; Translocation;
KW   Transport.
FT   CHAIN           1..969
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_1000144991"
FT   BINDING         99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         117..121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         631
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   969 AA;  110402 MW;  3D0CF20BBD92BB43 CRC64;
     MMDFLKRFFG SSQERILKRF QKLVEEVNAC DEKFSSLSDD ELREKTPQLK QRYQDGESLD
     KLLPEAYGVV KNVCRRLAGT PVEVSGYHQQ WDMVPYDVQI LGAIAMHKGF ITEMQTGEGK
     TLTAVMPLYL NALTGKPVHL VTVNDYLAQR DCEWVGSVLR WLGLTTGVLV SGSPPEKRKA
     IYQCDVVYGT ASEFGFDYLR DNSIATRKEE QVGRGFYFAI IDEIDSVLID EARTPLIISG
     PGEKHNPVYF ELKDRVAELV YFQREMCNHI AIEARKVLDP FLGTDVLPKD KKVMEAISEA
     CRALWLVSKG MPLNRVLRRV REHPDLRAMI DKWDVFYHAE QNKEECLEKL SSLYIVVDEH
     NNDFELTDKG MLQWIEKIGG AAEDFVMMDM GHEYALIEED ATLSPADKLN RKIAVSEKDT
     QRKARAHGLR QLLRAHLLME KDIDYIVRDD QIVIIDEHTG RPQPGRRFSE GLHQAIEAKE
     HVTIRKESQT FATVTLQNFF RLYEKLAGMT GTAITESREF KEIYSLYVLQ VPTFKPCLRI
     DHNDAFYMTE REKYQAIVAE IISAHRSGKP ILIGTESVEV SEKLSRILRQ NRINHTVLNA
     KNHAQEAEII AGAGKVGAVT VATNMAGRGT DIKLDEEAVA AGGLYVIGTS RHQSRRIDRQ
     LRGRCARLGD PGAAKFFLSF EDRLMRLFAS PKLNTLIRHF RPPEGEAMSD PMFDRLIETA
     QKRVEGRNYT IRKHTLEYDD VMNKQRQTIY AFRNDVLHAE DLFVVAKEQI EHVALALAFL
     ILKDAHADHC SLPKIEEWLS YSFPVKLDDQ EIRRLGDVDA VADYIGDLLI EAFDVKFSAM
     LAEFTEIIGS AANAQGICND ILRSVIISHI DEEWKVHLVD MDLLRSEVGL RSVGQKDPLI
     EFKNESFLLF EGLIRDIRIA IVKHLFALEL SLTRSDRPDN AIPTVATAFH NHDNFRPMEL
     TIVGEEEES
 
 
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