SECA2_MYCPA
ID SECA2_MYCPA Reviewed; 777 AA.
AC Q73ZR7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
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}; OrderedLocusNames=MAP_1534;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS03851.1; -; Genomic_DNA.
DR RefSeq; WP_003877905.1; NC_002944.2.
DR AlphaFoldDB; Q73ZR7; -.
DR SMR; Q73ZR7; -.
DR STRING; 262316.MAP_1534; -.
DR EnsemblBacteria; AAS03851; AAS03851; MAP_1534.
DR KEGG; mpa:MAP_1534; -.
DR PATRIC; fig|262316.17.peg.1625; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_2_11; -.
DR OMA; WADHLAF; -.
DR Proteomes; UP000000580; 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; Reference proteome; Translocase; Translocation;
KW Transport.
FT CHAIN 1..777
FT /note="Protein translocase subunit SecA 2"
FT /id="PRO_0000318381"
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; 85031 MW; 4F1ABC900ABB6872 CRC64;
MPKTNRAQPG RLSSRFWRLL GASTEKNRSR SLTLVTDSSE YDDEAAGLTD EQLRKAAGLL
NLEDLAESED IPQFLAIARE AAERATGLRP FDVQLLGALR MLAGDVIEMA TGEGKTLAGA
IAAAGYVLAG 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 RELADEIPEE
RLETICRHIM LYHLDRGWAD HLAYLADIRE SIHLRALGRQ NPLDEFHRLA VDAFASLAAD
AIEAAQQTFE TANVLEDEPG LDLSKLARPT STWTYMVNDN PLSDDTLSTL SLPGVFR