SECA_MYCPU
ID SECA_MYCPU Reviewed; 867 AA.
AC Q98RA6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=MYPU_1040;
OS Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=272635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAB CTIP;
RX PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT pulmonis.";
RL Nucleic Acids Res. 29:2145-2153(2001).
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 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}. Note=Distribution is 50-50.
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; AL445563; CAC13277.1; -; Genomic_DNA.
DR PIR; H90524; H90524.
DR RefSeq; WP_010924908.1; NC_002771.1.
DR AlphaFoldDB; Q98RA6; -.
DR SMR; Q98RA6; -.
DR STRING; 272635.MYPU_1040; -.
DR EnsemblBacteria; CAC13277; CAC13277; CAC13277.
DR KEGG; mpu:MYPU_1040; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_14; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR BioCyc; MPUL272635:G1GT6-103-MON; -.
DR Proteomes; UP000000528; 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; -; 3.
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; 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; PS51196; SECA_MOTOR_DEAD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW Protein transport; Reference proteome; Translocase; Translocation;
KW Transport.
FT CHAIN 1..867
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000320859"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 103..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 491
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 867 AA; 99775 MW; 2EAD598CFB6423B4 CRC64;
MIKKLKEIPF FKSTEMKIAE KTLQQINDLE PSVVNLTDEE LQNKTDEFVR RIQEGETLEH
IRPEVFAVSR EATKRVLKKR PYDVQMLGGI ILDLGSVAEM RTGEGKTITS IAPVYLNALE
KKGVIVSTVN EYLAERDAAE MGEVFSFLKM TVGVNKPSMS PEEKKQIYQC DITYSIHSEL
GFDYLRDNMV TNINDKVQRG LNYILLDEVD SILIDEARTP LIISGGESSS SYMYEVANQF
ARTLQPGDYE IDEESKTIKL VDSGIDKANK FFTLSNLYDI KNSELVHRIQ NALRANFIMK
KDVEYIVKDE KIELIDAFTG RIMEGRAYSE GLQQAIQAKE FLEIESETKT LATITYQNFF
RMFKKLSGMT GTAKTEEQEF IDIYNMRVNP IPTNLPNIRV DDEDSIYWGT RQKLNAILKE
VKQVSKTGQP ILIGTSQIEQ SEQLHQLFDQ NGIVHTVLNA KQNEQEANII SQAGQLNAIT
IATNMAGRGT DIKPSKEALA VGGLYVLGTD KSESRRIDNQ LRGRSGRQGD IGYSKFFLSL
DDQLILRFAG ADKLKEIFPK SEEALNSKQL KRHFSNAQKK IEGFNYDSRK TVLNYDDVIR
QQRELMYSQR DLILVSEDLL FVIERMVFRS VDDVLKNSMF LLKNGGFDYT KLTEYINDQW
LKPFDFKFEE SKLSHLHEKD LAEYIFQNLM EQYMIVRQRL IDSFGEDSIL YHERSILIST
IDSYWQNHIN SMDKLRSNSN MVQYAQKNPY QVYTQKGSKK FERLIVEIAL QSSVKLFNNP
SAYRQDQMEE VMIEGYTQEF IDKIPESERE YFKTLPQDLK SKIVKNLIQL EQSIAMVESN
DQSQDLQSIT IDILPDQNLN NSSDEAK
