SECA_PHYAS
ID SECA_PHYAS Reviewed; 832 AA.
AC B1VAB2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=PA0551;
OS Phytoplasma australiense.
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; 16SrXII (Stolbur group).
OX NCBI_TaxID=59748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18359806; DOI=10.1128/jb.01301-07;
RA Tran-Nguyen L.T., Kube M., Schneider B., Reinhardt R., Gibb K.S.;
RT "Comparative genome analysis of 'Candidatus Phytoplasma australiense'
RT (subgroup tuf-Australia I; rp-A) and 'Ca. Phytoplasma asteris' strains OY-M
RT and AY-WB.";
RL J. Bacteriol. 190:3979-3991(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 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; AM422018; CAM11885.1; -; Genomic_DNA.
DR RefSeq; WP_012359023.1; NC_010544.1.
DR AlphaFoldDB; B1VAB2; -.
DR SMR; B1VAB2; -.
DR STRING; 59748.PA0551; -.
DR EnsemblBacteria; CAM11885; CAM11885; PA0551.
DR KEGG; pal:PA0551; -.
DR eggNOG; COG0653; Bacteria.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000008323; 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..832
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000145040"
FT REGION 801..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 832 AA; 95819 MW; E2DEE63CAC217FC6 CRC64;
MFKFLKKIFN SSKKALRKAR VIANKVQNLT ETMSLLKDQD FVVKTNELKQ RYQKGETLNQ
LLPEAYALVR EATKRVTGLT PYYVQILGAI ILHQGNIAEM KTGEGKTLTA IMPAYLNALS
GDPVHIVTVN EYLAKREFEG KIGEVFLFLG LSVGINIKDN NTEEKQKAYL CDVLYTTNSE
LGFDYLRDNM EIDANNLVMK RPYSYAIIDE VDSILIDEAR TPLIISQSAK ETKNLYKEAN
RFVKTLKSKH YLIELESKTI ELTEEGINKA ESFFQIKNLY DVQHSSLLHH IKNALKAFFT
MHKNKDYLVN QNQVLIIDQF TGRVLKGRQF SDGLHQALEA KEGVLIKEET SIGATITYQN
FFRLYHKLSG MTGTAKTEED EFRDIYNMEV IEIPTNLPMI RVDEPDFIFV TIQEKYDALI
KTTLERHKLG QPILIGTTTV EVSEIISKKL AKNFIKHEIL NAKNHFKEAE IIAKAGLKNS
VTIATNMAGR GTDIRLGEGV ADLGGLAVLG TERHESRRID NQLRGRAGRQ GDPGYSRFFI
SSEDELAQRF GGKRIEKIIS LLQQINTSGK ETSSKMVTNF FTKIQKKVES SNFDYRKYLL
KYDDILRIQR EIIYDQRKGI LNSPHPEKIA LNLMEKTINQ AVVPFFTNTK KTNQPEELIL
FLEKSFFPKG TFDLKEVQAI FEQSPNTALT EFRKYLSNKM TVILEQQKDS FEKENNDINF
FDQVIRWFML KIIDNYYKRH INDMSVLRQG VGFVGYGQQD SFIEYQKEGQ ILFNKMVDQI
VMDITTAILR FPLPQSFQTP PQQEKMILND NNSDNNITKR RRKVRISKKP WN
