SECA2_LISMO
ID SECA2_LISMO Reviewed; 776 AA.
AC P0DJP3; Q2WCM9; Q2WCN0; Q8RLX5; Q8Y9E7;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 50.
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=lmo0583;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, AND
RP CHARACTERIZATION.
RC STRAIN=ATCC BAA-679 / EGD-e, SLCC7509, and SLCC7510;
RX PubMed=16321943; DOI=10.1128/jb.187.24.8385-8394.2005;
RA Machata S., Hain T., Rohde M., Chakraborty T.;
RT "Simultaneous deficiency of both MurA and p60 proteins generates a rough
RT phenotype in Listeria monocytogenes.";
RL J. Bacteriol. 187:8385-8394(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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: Knockout causes a smooth to rough phenotype
CC transition; cells grow as filaments longer than 10 um in length with
CC septa between cells but no indentations. Knockout also causes a smooth
CC to rough phenotype transition; cells grow as filaments longer than 10
CC um in length with septa between cells but no indentations
CC (PubMed:16321943, strain EGD-e). {ECO:0000269|PubMed:16321943}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; AM040041; CAJ01897.2; -; Genomic_DNA.
DR EMBL; AM040042; CAJ01898.2; -; Genomic_DNA.
DR EMBL; AL591975; CAC98662.1; -; Genomic_DNA.
DR PIR; AH1147; AH1147.
DR RefSeq; NP_464111.1; NC_003210.1.
DR RefSeq; WP_010989521.1; NZ_CP023861.1.
DR AlphaFoldDB; P0DJP3; -.
DR SMR; P0DJP3; -.
DR STRING; 169963.lmo0583; -.
DR PaxDb; P0DJP3; -.
DR PRIDE; P0DJP3; -.
DR EnsemblBacteria; CAC98662; CAC98662; CAC98662.
DR GeneID; 984550; -.
DR KEGG; lmo:lmo0583; -.
DR PATRIC; fig|169963.11.peg.602; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_9; -.
DR OMA; YYARQKE; -.
DR PhylomeDB; P0DJP3; -.
DR BioCyc; LMON169963:LMO0583-MON; -.
DR PHI-base; PHI:5255; -.
DR Proteomes; UP000000817; 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; -; 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; 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 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..776
FT /note="Protein translocase subunit SecA 2"
FT /id="PRO_0000318366"
FT BINDING 80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 98..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 486
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT VARIANT 32
FT /note="E -> D (in strain: SLCC7509 and SLCC7510)"
FT VARIANT 407
FT /note="E -> G (in strain: SLCC7510)"
FT VARIANT 553
FT /note="A -> T (in strain: SLCC7509)"
FT VARIANT 627
FT /note="I -> F (in strain: SLCC7510)"
FT VARIANT 674
FT /note="E -> D (in strain: SLCC7509)"
SQ SEQUENCE 776 AA; 89435 MW; 03B4BC6DF071449C CRC64;
MRQNYDDRKI VKQYREIARQ IVKKEGLYKN MEQAELCEQT NFWREKFKTK PMTDRDKINI
FALAREAASR IIGLDAVVVQ LIGALVLGDG KVAEMKTGEG KTLMSLFVMF IEVMRGNRVH
LVTANEYLAR RDREEIGQVL EYLGVSVALN ESGLDIAQKK AIYTADVIYG TASEFGFDYL
RDNMVRQKED KVQSGLDFVL IDEADSILID EARTPLLISD RKEEDLSLYH TANKLVKKMM
KDDYEMEEHK RFVWLNDAGI EKAQKFWGVE SLYSAEAQSE LRITMLLMRA HFLMHKDKDY
VVLDDEVLII DPHTGRALPG RRFNDGLHQA IEAKEGVEVK EESRTLATIT IQNYFRMYKK
ISGMTGTAKT EEEEFRQIYN MDVVVIPTNL RVNREDMQDD IFYTKKEKGR AIVYEVSWRY
EKGQPTLIGT SSIKSNEWIS GLLDAAGIPH QVLNAKNHAQ EAEIIAKAGK RGMVTLATNM
AGRGTDIKLD PDVHKLGGLA VIGTERHESR RIDLQLMGRS GRRGDPGFSK FMISLEDDLL
EQFESKSWEK LSAKLKRKAP RDGKPVNSRK IHAVVVDAQK RLEGANYDIR KDLLSYDEVI
DLQRKMVYKE RDLLLERNKL GVSSEKILRE VAEYSFIHPS DIPEEELEIY YSRQKELLGG
TKFPISFDQV TLMEPREVVE EIVSWHKKER NKFPAETIAA IEREVYLNLM DQMWVMHLDA
MVQLREGIHL RAYGQQDPLV MYQKEGAQLF EKFQADYHFY FAHALLELDP DGLIQG
