ID A0A0C2JK56_9ACTN Unreviewed; 986 AA.
AC A0A0C2JK56;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Protein translocase subunit SecA {ECO:0000256|HAMAP-Rule:MF_01382, ECO:0000256|RuleBase:RU003874};
DE EC=7.4.2.8 {ECO:0000256|HAMAP-Rule:MF_01382};
GN Name=secA {ECO:0000256|HAMAP-Rule:MF_01382};
GN ORFNames=LP52_08165 {ECO:0000313|EMBL:KIH99330.1};
OS Streptomonospora alba.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Streptomonospora.
OX NCBI_TaxID=183763 {ECO:0000313|EMBL:KIH99330.1, ECO:0000313|Proteomes:UP000031675};
RN [1] {ECO:0000313|Proteomes:UP000031675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 90003 {ECO:0000313|Proteomes:UP000031675};
RX PubMed=25601074; DOI=10.1016/j.chembiol.2014.11.017;
RA Metelev M., Tietz J.I., Melby J.O., Blair P.M., Zhu L., Livnat I.,
RA Severinov K., Mitchell D.A.;
RT "Structure, bioactivity, and resistance mechanism of streptomonomicin, an
RT unusual lasso Peptide from an understudied halophilic actinomycete.";
RL Chem. Biol. 22:241-250(2015).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_01382};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:0000256|HAMAP-Rule:MF_01382}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01382};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01382};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01382}. Cytoplasm
CC {ECO:0000256|HAMAP-Rule:MF_01382}. Note=Distribution is 50-50.
CC {ECO:0000256|HAMAP-Rule:MF_01382}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000256|ARBA:ARBA00007650,
CC ECO:0000256|HAMAP-Rule:MF_01382, ECO:0000256|RuleBase:RU003874}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIH99330.1}.
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DR EMBL; JROO01000013; KIH99330.1; -; Genomic_DNA.
DR RefSeq; WP_040272117.1; NZ_JROO01000013.1.
DR AlphaFoldDB; A0A0C2JK56; -.
DR STRING; 183763.LP52_08165; -.
DR OrthoDB; 9805579at2; -.
DR Proteomes; UP000031675; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; cd17928; DEXDc_SecA; 1.
DR CDD; cd18803; SF2_C_secA; 1.
DR Gene3D; 3.10.450.50; -; 1.
DR Gene3D; 1.10.3060.10; Helical scaffold and wing domains of SecA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.90.1440.10; SecA, preprotein cross-linking domain; 1.
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; IPR004027; SEC_C_motif.
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; IPR011116; SecA_Wing/Scaffold.
DR InterPro; IPR036266; SecA_Wing/Scaffold_sf.
DR InterPro; IPR036670; SecA_X-link_sf.
DR NCBIfam; TIGR00963; secA; 1.
DR PANTHER; PTHR30612:SF0; CHLOROPLAST PROTEIN-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR30612; SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM; 1.
DR Pfam; PF21090; P-loop_SecA; 1.
DR Pfam; PF02810; SEC-C; 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; SSF81886; Helical scaffold and wing domains of SecA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF81767; Pre-protein crosslinking domain of SecA; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01312; SECA; 1.
DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01382};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01382};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01382};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01382};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01382};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW Rule:MF_01382}; Reference proteome {ECO:0000313|Proteomes:UP000031675};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_01382};
KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW Rule:MF_01382};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01382};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 2..615
FT /note="SecA family profile"
FT /evidence="ECO:0000259|PROSITE:PS51196"
FT DOMAIN 88..246
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 418..620
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 866..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 104..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ SEQUENCE 986 AA; 109103 MW; 20B3E913D54434C4 CRC64;
MPAILDKVLR AGEGKILRKL NKLKDQINSI EDDFVDLSDG ELRELTDELR QRHKDGESLD
DLLPEAFAAV REAAKRTLGQ RHFDVQLMGG AALHLGNIAE MKTGEGKTLT SALAVYLNAL
AGEGAHVVTP NDYLAKRDAE NMGRIYQFLG MKVGVLAPEM PRTERQAAYA ADITYGTNNE
FGFDYLRDNM AVSLEETVQR GHSYAIVDEV DSILIDEART PLIISGPAEQ NSKWYSEFAK
IAPRLVRDTD YEVEEKNRTV GITESGVAKV EDWLGIDNLY ESVNTPLISF LNNALKAKEL
YRRDKEYIVK DGEVLIVDEF TGRVLRGRRY NEGMHQAIEA KERVQIKDEN QTQAKITLQN
YFRLYSKLAG MTGTAVTEAA EFDQTYGIGV VAIPTNKPMI RSDERDVIYK GEDAKFEAVV
DDIAECNENG QPVLVGTTSV EKSELLSKML KRRGIAHEVL NAKNHAREAS IIARAGKLGA
VTVATNMAGR GTDIMLGGNP EFMADEELQR RGLSPLETSE EYEEAWPEAL EKAKKEVESE
HEQVVEAGGL YVLGTERHES RRIDNQLRGR SGRQGDPGLS RFYLSLEDDL MRLFNSGRVE
LIYERLNIPD DQPIESKVVT KAIQSAQAQV EAQNLEIRKN VLKYDEVLNR QRKVIYAERR
KVLEGADLRE QASGMLDDVL DGYVRAATNE GDAGDWDLDR LWQAFKQIYP ISFSVDDLIE
ENGGEVTAVT PDVISERVLE DAHAAYARRE EELGSEAMRE LERRVILEVM GRKWREHLYE
MDYLQQGIGL RAMAQRNPLI EYQREGFDMF QEMLEAIKEE SVGYLFNVEV QVRGKTSASV
TPASAAVTAA GAAGGAVVTA APAEGGVATK EAGEEDEADK VLGGKPSDSA KPDAEDVVEA
EAAADHEAAA DKDALDDGGE ELVVSGFGQS RPSRLQYSAP AEDGTVDTRT ETVEDAYAGA
SRNAPCPCGS GKKFKKCHGD PRNRTA
//
