ID   A0A4Q9RPA0_9FLAO        Unreviewed;      1117 AA.
AC   A0A4Q9RPA0;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   02-JUN-2021, entry version 7.
DE   RecName: Full=Protein translocase subunit SecA {ECO:0000256|HAMAP-Rule:MF_01382, ECO:0000256|RuleBase:RU003874};
GN   Name=secA {ECO:0000256|HAMAP-Rule:MF_01382};
GN   ORFNames=DMZ43_11050 {ECO:0000313|EMBL:TBV25479.1};
OS   Meridianimaribacter sp. CL38.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Meridianimaribacter; unclassified Meridianimaribacter.
OX   NCBI_TaxID=2213021 {ECO:0000313|EMBL:TBV25479.1, ECO:0000313|Proteomes:UP000293797};
RN   [1] {ECO:0000313|EMBL:TBV25479.1, ECO:0000313|Proteomes:UP000293797}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL38 {ECO:0000313|EMBL:TBV25479.1,
RC   ECO:0000313|Proteomes:UP000293797};
RA   Lam M.Q., Oates N.C., Thevarajoo S., Goh K.M., Bruce N.C., Chong C.S.;
RT   "Genome sequencing of Meridianimaribacter sp. CL38.";
RL   Submitted (JUN-2018) 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   -!- 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:TBV25479.1}.
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DR   EMBL; QKWS01000004; TBV25479.1; -; Genomic_DNA.
DR   Proteomes; UP000293797; 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: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   HAMAP; MF_01382; SecA; 1.
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; 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; TIGR00963; secA; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01382};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01382};
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};
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}.
FT   DOMAIN          5..770
FT                   /note="SECA_MOTOR_DEAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51196"
FT   NP_BIND         192..199
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT   REGION          1031..1064
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          64..84
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1031..1051
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1117 AA;  127058 MW;  A07F4DBE60B82963 CRC64;
     MSFLDSVLKV FVGDKSKQDV KSITPIVDKI KTFASALEQL SHDELRAKTD AFKAKIAEAR
     QPLLEKKEQL LKQAETTEDI DEREDIYVEA DKIEDDIYQV TEDVLNDILP EAFAVVKETA
     KRFVSNTEIT VTASTFDREL SGSKEYITLE DDKAVWSNSW DAAGKAITWD MVHYDVQLIG
     GVAMHQGKIA EMQTGEGKTL VATLPVYLNA LAGKGVHLVT VNDYLAKRDS AWMAPIFEFH
     GLSVDCIDYH QPNSAARKKA YMADITYGTN NEFGFDYLRD NMAHSPDDLV QRPHHYAIVD
     EVDSVLVDDA RTPLIISGPI PQGDRHEFTE LKPKVDNIAG VQRKMLTGVL AEAKKLIAEG
     DTKEGGFLLL RVYRGMPKNK ALIKFLSEEG IKQLLQKTEN YYMQDNNREM PKIDAELYYV
     IDEKNNQVEL TDKGVEFLSG EDDPNFFVMP EIGVEIAKIE AQGLSKEEEA EAKEDLFRDF
     GVKSERIHTL NQLLKAYALF EKDIQYVVMD NKVMIVDEQT GRIMDGRRYS DGLHQAIEAK
     ENVKIEDATQ TFATVTLQNY FRMYRKLSGM TGTAVTEAGE FWEIYKLDVV EIPTNKPIAR
     DDREDLVYKT KREKYNAVID EVTALSQAGR PVLIGTTSVE ISELLGKMLS IRKVPHNVLN
     AKLHKKEADI VAEAGKAGQV TIATNMAGRG TDIKLSEDVK AAGGLAIVGT ERHDSRRVDR
     QLRGRAGRQG DPGSSQFYVS LEDNLMRLFG SERIAKMMDR MGLQEGEVIQ HSMISKSIER
     AQKKVEENNF GVRKRLLEYD DVMNAQREVV YKRRHHALFG ERLRVDLANM IYDTSEGIAQ
     TNKDANDFKN FEFELIRYFS MSSPITEAEF SKLSTQDIAG KIYKAAFEHY REKMERNAEI
     AFPVIKNVYE NQRDKFKRIV VPFTDGVKNL QVVTDLEKAY ETNGKQLIND FEKNITLAIV
     DDSWKTHLRK MDELKQSVQL AVHEQKDPLL IYKFEAFELF KQMLDQVNKD VISFLFKGEL
     PTETQNTIQE ARARRKENLE TSKEEIPNMD ERSAQNRAAG NTQRQPEVIE TIVRDKPKIG
     RNDKVTIKHV MSGENKTVKY KQAEPLIAKG EWVLIEE
//