SECA2_MYCS2
ID SECA2_MYCS2 Reviewed; 784 AA.
AC A0QYG9; I7FEY4; Q9EZL3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Protein translocase subunit SecA 2 {ECO:0000255|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA2 {ECO:0000255|HAMAP-Rule:MF_01382};
GN OrderedLocusNames=MSMEG_3654, MSMEI_3567;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=11717254; DOI=10.1128/jb.183.24.6979-6990.2001;
RA Braunstein M., Brown A.M., Kurtz S., Jacobs W.R. Jr.;
RT "Two nonredundant SecA homologues function in mycobacteria.";
RL J. Bacteriol. 183:6979-6990(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
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.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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 -!- DISRUPTION PHENOTYPE: Not essential, the disruption mutant is super-
CC sensitive to azide, export of some proteins is decreased and has a
CC small colony growth phenotype on rich agar medium. It cannot replace
CC secA1. {ECO:0000269|PubMed:11717254}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; AF287049; AAG44890.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK70947.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP40030.1; -; Genomic_DNA.
DR RefSeq; WP_011729234.1; NZ_SIJM01000008.1.
DR RefSeq; YP_887957.1; NC_008596.1.
DR AlphaFoldDB; A0QYG9; -.
DR SMR; A0QYG9; -.
DR STRING; 246196.MSMEI_3567; -.
DR PRIDE; A0QYG9; -.
DR EnsemblBacteria; ABK70947; ABK70947; MSMEG_3654.
DR EnsemblBacteria; AFP40030; AFP40030; MSMEI_3567.
DR GeneID; 66735036; -.
DR KEGG; msg:MSMEI_3567; -.
DR KEGG; msm:MSMEG_3654; -.
DR PATRIC; fig|246196.19.peg.3601; -.
DR eggNOG; COG0653; Bacteria.
DR OMA; WADHLAF; -.
DR OrthoDB; 212453at2; -.
DR BRENDA; 7.4.2.5; 3445.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW Protein transport; Reference proteome; Translocase; Translocation;
KW Transport.
FT CHAIN 1..784
FT /note="Protein translocase subunit SecA 2"
FT /id="PRO_0000318382"
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"
FT CONFLICT 1
FT /note="M -> MANESWRTSAYRKRV (in Ref. 1; AAG44890)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 784 AA; 85424 MW; 869122A8397C6691 CRC64;
MPKTSSAKPG RLSSKFWKLL GASTERNQAR SLSEVKGAAD FEKKAADLDD EQLTKAAKLL
KLEDLAGASD ITQFLAIARE AAERTTGLRP FDVQLLAALR MLAGDVVEMA TGEGKTLAGA
IAAAGYALGG RRVHVITIND YLARRDAEWM GPLLKALGLT VGWITADSTA DERREAYQCD
VTYASVNEIG FDVLRDQLVT DVADLVSPNP DVALIDEADS VLVDEALVPL VLAGTSHREQ
PRVEIIRMVG ELEAGKHYDT DAESRNVHLT EAGARVMEAK LGGIDLYSEE HVGTTLTEIN
VALHAHVLLQ RDVHYIVRDD AVHLINASRG RIASLQRWPD GLQAAVEAKE GIETTETGEV
LDTITVQALI NRYPRVCGMT GTALAAGEQL RQFYKLGVSP IPPNTPNIRK DEPDRVYITA
AAKIDAIVEH IAEVHKTGQP VLVGTHDVAE SEELHEKLLK AGVPAVVLNA KNDAEEAAVI
AEAGKLGAVT VSTQMAGRGT DIRLGGSDVG DDDAEKKKVA ELGGLHVVGT GRHHTERLDN
QLRGRAGRQG DPGSSVFFSS WEDDVVAAHL ERSKLPMETD PDAGDGRIIA PRAASLLDHA
QRVAEGRLLD VHANTWRYNQ LIAQQRAIIV ERRETLLRTD TAREELKERS PERYAKLAEE
LGEDAEERLE KICRLIMLYH LDRGWCEHLA FLADIRESIH LRALGRQNPL DEFHRMAVDA
FASLAADAIE AAQQTFETAE SVADEPGVDL SKLARPTSTW TYMVHDNPLA DDTMSALSLP
GVFR
