ID   H1YEF6_9SPHI            Unreviewed;      1159 AA.
AC   H1YEF6;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Protein translocase subunit SecA {ECO:0000256|HAMAP-Rule:MF_01382};
DE            EC=7.4.2.8 {ECO:0000256|HAMAP-Rule:MF_01382};
GN   Name=secA {ECO:0000256|HAMAP-Rule:MF_01382};
GN   ORFNames=Mucpa_3086 {ECO:0000313|EMBL:EHQ27190.1};
OS   Mucilaginibacter paludis DSM 18603.
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=714943 {ECO:0000313|EMBL:EHQ27190.1, ECO:0000313|Proteomes:UP000002774};
RN   [1] {ECO:0000313|EMBL:EHQ27190.1, ECO:0000313|Proteomes:UP000002774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18603 {ECO:0000313|EMBL:EHQ27190.1,
RC   ECO:0000313|Proteomes:UP000002774};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Held B.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The permanent draft genome of Mucilaginibacter paludis DSM 18603.";
RL   Submitted (SEP-2011) 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:0000256|HAMAP-Rule:MF_01382}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(2)O + cellular protein(Side 1) = ADP + phosphate +
CC         cellular protein(Side 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM001403; EHQ27190.1; -; Genomic_DNA.
DR   STRING; 714943.Mucpa_3086; -.
DR   EnsemblBacteria; EHQ27190; EHQ27190; Mucpa_3086.
DR   eggNOG; COG0653; Bacteria.
DR   HOGENOM; CLU_005314_0_0_10; -.
DR   OrthoDB; 212453at2; -.
DR   Proteomes; UP000002774; 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: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; 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; 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   PANTHER; PTHR30612; PTHR30612; 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; SM00490; HELICc; 1.
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; 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}; Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
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:UP000002774};
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..829
FT                   /note="SECA_MOTOR_DEAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51196"
FT   DOMAIN          177..336
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          682..845
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   NP_BIND         193..197
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT   REGION          667..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1083..1108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1087..1105
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         175
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT   BINDING         751
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   1159 AA;  130526 MW;  B92A6CEE1EF62E65 CRC64;
     MLGFISKLFG NKSDRDVKTI QPIVEKIKAE FAKLGTLSND ELRAKTLDFK ERIKNGLADI
     DAALQSVKTQ AENPDLDVSE KVDLYTQIDK IEKDRNKELE VILLQILPEA FAVVKETAKR
     FTENKTIEVT ATPFDRELAA IKKNVIINGD KAVHHNSWIA AGNEVTWNMV HYDVQLLGGV
     VLHQGKIAEM ATGEGKTLVA TLPAYLNAIA GEGVHIVTVN DYLARRDSEW MGPLYEFHGL
     SVDCIDRHEP NSEERRNAYL ADITFGTNNE FGFDYLRDNM TRSPEELVQR KLHYAMVDEV
     DSVLIDDART PLIISGPIPR GDEHEFYELK PRIERLVNTQ KNYVLGVLNE AKKLINDGKT
     GVEDGGLALL RAHRGLPKNK ALIKFLSEGG NKTILQKTEN YYMQDSAKEM PKVDAELYFI
     IDEKNNQVEL SEKGIELITT SGEDPHFFVM PDVGGEVADI EKSALTIEEK VAKKDALMRD
     FSIKSERIHS INQLLKAYTL FEKDVEYILD EGKVKIVDEQ TGRVLDGRRY SDGLHQAIEA
     KENVKVEDAS QTFATVTLQN YFRMYHKLCG MTGTAVTEAG EFWEIYKLDV VEIPTNTPTS
     RSDYQDLVYR TVREKYNAVA GEIQTLVFPY SHYEPQYEKD KEGKIKMSAG KPVVKFDSAG
     KPVPQLDGKG SLIPAPNPLT GQLEPRAGRP VLVGTTSVEI SELLSRMLKL RGIKHNVLNA
     KMHQKEADIV AEAGKSGTVT IATNMAGRGT DIKLGEGVKD VGGLAIVGTE RHESRRVDRQ
     LRGRAGRQGD PGSSQFFVSL EDDLMRLFGS ERISSLMVKM GIEEGEVIQH SMITNSIERA
     QKKVEENNFG IRKRLLEYDD VMNSQRTVIY TKRKNALFGE RLDVDLSNTI FDVADDVVAE
     YKGENNYEGF KLEVIRLFSL DVDISEDEFA SLSANKLTDK TFHQVTDFYK RKAEAIANQA
     YPVLKDVYDN RQGIENIIVP FTDGIHGLQI AVPLKKAIDN HGQEVFKSFE KNVTLTFIDD
     AWKEHLREMD ELKQSVQNAV YEQKDPLLVY KFEAFELFRQ MLANVNKEIV SFLFRGGIPM
     QQEEEVQEAR PQPKTDMRNM RTSKPELAHE TNGVPTLVDD TREVQKQMPV KAEQKIGRND
     PCPCGSGKKF KNCHGVGVA
//