SECA_MYCA1
ID SECA_MYCA1 Reviewed; 777 AA.
AC A0QGP2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=MAV_2894;
OS Mycobacterium avium (strain 104).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=243243;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- MISCELLANEOUS: This Mycobacterium is unusual in only having an intact
CC secA2 gene. The secA1 gene, which is essential in MYCS2, is annotated
CC as a pseudogene in this organism (MAV_4203).
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; CP000479; ABK65479.1; -; Genomic_DNA.
DR RefSeq; WP_009977026.1; NC_008595.1.
DR AlphaFoldDB; A0QGP2; -.
DR SMR; A0QGP2; -.
DR EnsemblBacteria; ABK65479; ABK65479; MAV_2894.
DR KEGG; mav:MAV_2894; -.
DR HOGENOM; CLU_005314_3_2_11; -.
DR OMA; WADHLAF; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000001574; 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; IPR026389; SecA_Actinobact_type.
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; TIGR04221; SecA2_Mycobac; 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; Translocase; Translocation; Transport.
FT CHAIN 1..777
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000318377"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 112..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 501
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 777 AA; 85017 MW; 4AF3B4FE63170C59 CRC64;
MPKTNRAQPG RLSSRFWRLL GASTEKNRSR SLTLVTDSSE YDDEAAGLTD EQLRKAAGLL
NLEDLAESED IPQFLAIARE AAERATGLRP FDVQLLGALR MLAGDVIEMA TGEGKTLAGA
IAAAGYALAG RHVHVVTIND YLARRDAEWM GPLIEAMGLT VGWITAESSS EERRAAYGCD
VTYASVNEIG FDVLRDQLVT DVADLVSPNP DVALIDEADS VLVDEALVPL VLAGTTHRET
PRLEIIKLVG ELEAGTDYDT DADSRNVHLT DVGARKVEKA LGGIDLYSEE HVGTTLTEVN
VALHAHVLLQ RDVHYIVRDD AVHLINASRG RIAQLQRWPD GLQAAVEAKE GIETTETGEV
LDTITVQALI NRYATVCGMT GTALAAGEQL RQFYKLGVSP IPPNKPNIRE DEADRVYITA
AAKNDAIVEH IIEVHETGQP VLVGTRDVAE SEELHERLLR RGVPAVVLNA KNDAEEAQVI
AEAGKFGVVT VSTQMAGRGT DIRLGGSDEA DHDRVAELGG LHVVGTGRHH TERLDNQLRG
RAGRQGDPGS SVFFSSWEDD VVAANLDRNK LPMETDPETG DGRIVSPKAA GLLDHAQRVA
EGRMLDVHAN TWRYNQLIAQ QRAIIVDRRN TLLRTATARE ELAELAPKRY RELAEEIPEE
RLETICRHIM LYHLDRGWAD HLAYLADIRE SIHLRALGRQ NPLDEFHRLA VDAFASLAAD
AIEAAQQTFE TANVLEDEPG LDLSKLARPT STWTYMVNDN PLSDDTLSTL SLPGVFR
