SECA_UREPA
ID SECA_UREPA Reviewed; 837 AA.
AC Q9PR25;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=UU119;
OS Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=273119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700970;
RX PubMed=11048724; DOI=10.1038/35037619;
RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA Cassell G.H.;
RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL Nature 407:757-762(2000).
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; AF222894; AAF30525.1; -; Genomic_DNA.
DR RefSeq; WP_006689106.1; NC_002162.1.
DR AlphaFoldDB; Q9PR25; -.
DR SMR; Q9PR25; -.
DR STRING; 273119.UU119; -.
DR EnsemblBacteria; AAF30525; AAF30525; UU119.
DR GeneID; 29672143; -.
DR KEGG; uur:UU119; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_14; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000000423; 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..837
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000073495"
FT BINDING 83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 101..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 494
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 837 AA; 96317 MW; A5319B46438F6787 CRC64;
MNLISKISPQ NRILNRARLI AEEVLKKEEE YEHFSDQELI NKSDDIIEYL ANNNPLDDKL
VEALCIIREV IYRVHNKRAF KVQIIGAIIV YFGDFAEMMT GEGKTLTLVL VAYLNALYKK
GVHMVTVNEY LVKVGAEFAT PVLNFLNMSV GQITANMNEY EKRNNYNCDI TYTTNSELGF
DYLRDNMVTN YANKVQRGLW FAIVDEGDSV LIDEARTPLI ISGEPQEEIG NYVKADRFVK
TLYPQDFTLD PESQSVALTE SGVEKAQKFF NTKNYYNFEN SDIIHKVTNA LRANFTFFNG
REYIVKKDDD GEDIIALVDQ STGRIMEGRS YSAGLQQAIQ AKEQIKIEPE NLTVATITYQ
SLFRLYKKLA AVSGTAITEA EEFLNIYNMV VVTIPTNKPI KRIDHPDYVF DNKRTKWKYV
IADVIRRHEN GQPILIGTAS VEDSEILHQL LERVNIPHEV LNAKNHAREA EIIACAGEYK
AVTIATNMAG RGTDIKLSPE SLEAGGLCVI GTERSDSRRI DNQLRGRAGR QGDIGESRFF
ISMEDTLFSR FATDNLAKAD DKLSEDVIST KFFTRLLNNT QKKVESLNYD TRKNLIDYDH
VLSNQRELIY KQRDKILISS DNKDILYRML DSVIDDLIYQ SHNKPNEDII DIKKLIDLAT
QNIFYDNYLN QDEYYGLKFE QIKTKLKKDC INFFEQKEQL MTPTIFNQIL SEIMISNIDE
EWTKHLDITS KIREGVNLRA YEQKAPLNIY VEDSDKLFEK LKHNVAWKTV CSIGKINYVH
QDYSDLNSEF IVNDNEINEN NNSIDFENFN ESIPTDQTIQ ESFDDNQSDN EDDKNNN
