SECA_MYCPN
ID SECA_MYCPN Reviewed; 808 AA.
AC P75559;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=MPN_210;
GN ORFNames=MP621;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB96269.1; -; Genomic_DNA.
DR PIR; S73947; S73947.
DR RefSeq; NP_109898.1; NC_000912.1.
DR RefSeq; WP_010874567.1; NC_000912.1.
DR AlphaFoldDB; P75559; -.
DR SMR; P75559; -.
DR IntAct; P75559; 3.
DR STRING; 272634.MPN_210; -.
DR PRIDE; P75559; -.
DR EnsemblBacteria; AAB96269; AAB96269; MPN_210.
DR KEGG; mpn:MPN_210; -.
DR PATRIC; fig|272634.6.peg.229; -.
DR HOGENOM; CLU_005314_3_0_14; -.
DR OMA; MVHYDVQ; -.
DR BioCyc; MPNE272634:G1GJ3-340-MON; -.
DR Proteomes; UP000000808; 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; 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 membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW Protein transport; Reference proteome; Translocase; Translocation;
KW Transport.
FT CHAIN 1..808
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000109596"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 105..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 808 AA; 91810 MW; E768F0B8915F892F CRC64;
MGLFNFLKLV SPRHRIYHKA SKIANEVEGH KNYYRNLTDV QLLEESNKLV DLVTKQNYTI
LDVAVAALAL IREVVYRETG EFAYRVQIIG AYIVLIGDFA EMMTGEGKTL TIVLAAYVSA
LEKRGVHVVT VNEYLAQRDA TNATKILKRV GMTVGCNFAN LAPHLKQAAF ACDVTYTTNS
ELGFDYLRDN MVHRFEDKKI RELHFAIVDE GDSVLIDEAR TPLIISGPAK NEFAAYVAVD
RFVKKLKEDE YKIDPESRAP ALTELGIKHA EKNFKTDNLF ALENSDLFHK IINALTAVKV
FEQGKEYIVR DGKVLIVDHF TGRILEGRSY SNGLHQAVQA KEMVEIEPEN VIVATITYQS
FFRLYNRLSA VSGTAFTESE EFLKIYNMVV VPVPTNRPNI RKDRADSVFG TPNIKWLAVV
KEVKRIHETG RPILIGTANI DDSELLHNYL QEANIPHEVL NAKNHSREAE IVAKAGQKGA
VTISTNMAGR GTDIRLGEGV AEMGGLYVLG TERNESRRID NQLRGRAGRQ GDRGETKFFI
SLGDALFKRF AHDRIERAIT KLGNDTFDSS FFSKMLSRTQ KRVEAINFDT RKNLIDYDHV
LASQRELIYK QRDKFLLATD LSDMIDKMLE KFVEQFCDQY RNPKNQNLVN HIALSEALNL
ELNMHGVISP KLFENMTFDA TVHKTHSLIG EKITNKVKVL TPPIALIRFR EIMITAMDKH
WIEHLDNVFK LREGVTLRSM EQTSPLNVYI RETDILFQTM LQKIARDVII QIANLATPEE
FDEELMKANA LKKLQALREA HEKSNEGQ
