SECA3_MYCVP
ID SECA3_MYCVP Reviewed; 785 AA.
AC A1T9W4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Protein translocase subunit SecA 3 {ECO:0000255|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA3 {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=Mvan_3162;
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-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 -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABM13964.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000511; ABM13964.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041307902.1; NC_008726.1.
DR AlphaFoldDB; A1T9W4; -.
DR SMR; A1T9W4; -.
DR STRING; 350058.Mvan_3162; -.
DR EnsemblBacteria; ABM13964; ABM13964; Mvan_3162.
DR KEGG; mva:Mvan_3162; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_2_11; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000009159; 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..785
FT /note="Protein translocase subunit SecA 3"
FT /id="PRO_0000318394"
FT BINDING 98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 116..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 505
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 785 AA; 85834 MW; 3F2B3A7D44F94E3D CRC64;
MARTSSKTDS PKTGRLSGRF WKLLGASTDK DQARSMAQVH KAAEFDAKAA DLDDEQLRKA
ARLLELDDLA DSTDVPQFLA IAREAAKRTT GLTPFDVQLQ GALRMLAGDV VEMATGEGKT
LSGAIAAAGY ALAGRNVHVI TINDYLARRD AEWMGPLIEA MGLTIGWITA DSTAAERRAA
YRCDITYASV NEIGFDVLRD QLVTDVDDLV SPNPDVALID EADSVLVDEA LVPLVLAGTS
HRETPRLELI RLVGELDENT DFATDNDSRN VHLTEAGARK IEAALGGIDL YSEEHVATTL
TEVNVALHAH VLLQRDVHYI VRDDAVHLIN SSRGRIATLQ RWPDGLQAAV EAKEGIETTE
TGEVLDTITV QALINRYPRV CGMTGTALAA GEQLRQFYKL GVSPIPPNKP NIRQDETDRV
YVTIAAKNDA VIEHIAEVHE TGQPVLVGTR DVAESEEIHR RLVKAGVPAV VLNAKNDAEE
AAVIAEAGKL GAVTVSTQMA GRGTDIRLGG SDEEDHDRVA ELGGLHVIGT GRHHTERLDN
QLRGRAGRQG DPGSSVFFSS WEDDLVMSHL EDNKLPLECD ETGRVISPKA ATLLEHAQRV
AEGRLLDVHA NTWRYNQLIA QQRAILVERR NTLLRTTTAR DEIAELVPER YEEVKARLTA
KDSETGEAKL ETICRLIMLY HLDRAWADHL AFLADIRESI HLRALGRQNP LDEFHRMAVD
AFASLAADAI EAAQQTFETA PSIEDEPGVD LSKLARPTST WTYMVHDNPL ADDTLSALSL
PGVFR
