SECA2_RHOBA
ID SECA2_RHOBA Reviewed; 657 AA.
AC Q7UWI5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 103.
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=RB2013;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01382}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}.
CC Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-
CC 50. {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=CAD72378.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BX294136; CAD72378.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_864696.1; NC_005027.1.
DR AlphaFoldDB; Q7UWI5; -.
DR SMR; Q7UWI5; -.
DR STRING; 243090.RB2013; -.
DR EnsemblBacteria; CAD72378; CAD72378; RB2013.
DR KEGG; rba:RB2013; -.
DR PATRIC; fig|243090.15.peg.918; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_2_0; -.
DR InParanoid; Q7UWI5; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015462; F:ABC-type protein transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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 GO; GO:0043952; P:protein transport by the Sec complex; IBA:GO_Central.
DR CDD; cd18803; SF2_C_secA; 1.
DR Gene3D; 3.40.50.300; -; 2.
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; IPR036670; SecA_X-link_sf.
DR PANTHER; PTHR30612; PTHR30612; 1.
DR Pfam; PF07517; SecA_DEAD; 1.
DR Pfam; PF01043; SecA_PP_bind; 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 PROSITE; PS01312; SECA; 1.
DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm; Membrane;
KW Nucleotide-binding; Protein transport; Reference proteome; Translocase;
KW Translocation; Transport.
FT CHAIN 1..657
FT /note="Protein translocase subunit SecA 2"
FT /id="PRO_0000318417"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 111..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 531
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 657 AA; 74268 MW; 72279283C86EE07F CRC64;
MRRSSDPSAN KKKWTKASNW RPRMVRWQRQ LARVNALEST LQAEDDQTIR KRSLALRYRA
MAGEKLSELL PEAYALCREA GRRSLSMRHY DVQILGGIAL FEGHITEMQT GEGKTLTATL
PLYLHSLVGK GAHLATVNDY LAKRDAEWMM PLFEMLGVSV GIIQTEDDQG GRRKSYGAAI
TYGTAKEFGF DFLRDRLLLR AQNRMQTEML GSGDGGFSNS GDQVVMRGMH FCLVDEADSI
LIDEARTPLI IGSIEDTVRD QIIETYKWAA ENAPLFELDE HFEIDDETKR YELTARGRSK
VRALPKSDLV RTMGLVDMYE YIERSIKTHR EFLLDRQYVI RPSEKDPNVD EIVIVDEFTG
RLAEGRKWRD GIHQSIEAKE GVEISVPTGQ AARITVQDLF LRYPHLAGMT GTAATSAGEL
RKIYRTPVVR VPTNRPPQRI QLPSRVFGTL TSKFEAIAKE VEEIHATGRP VLVGTRSIDK
SVLLSKLLDD LGIEHEVLNA NNVEREAEIV AEAGGRGKVT VATNMAGRGT DIKLSNDVEQ
IGGMHVICTE LHDAARIDRQ LIGRCGRQGD RGSYRQYLSL DDDILKGGYG AIKYEKLKKR
GEATSGSVDR LAAMFHKAQR KVERRHFRDR MVLMHHEKER KKMQREIGQD PYLDTPD
