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Database: UniProt
Entry: A0A0M1JAN1_9GAMM
LinkDB: A0A0M1JAN1_9GAMM
Original site: A0A0M1JAN1_9GAMM 
ID   A0A0M1JAN1_9GAMM        Unreviewed;       279 AA.
AC   A0A0M1JAN1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Cell division protein FtsY {ECO:0000313|EMBL:KOR29785.1};
DE   Flags: Fragment;
GN   ORFNames=TI04_07775 {ECO:0000313|EMBL:KOR29785.1};
OS   Achromatium sp. WMS2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Achromatium.
OX   NCBI_TaxID=1604835 {ECO:0000313|EMBL:KOR29785.1, ECO:0000313|Proteomes:UP000037003};
RN   [1] {ECO:0000313|EMBL:KOR29785.1, ECO:0000313|Proteomes:UP000037003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WMS2 {ECO:0000313|EMBL:KOR29785.1};
RX   PubMed=26322031; DOI=10.3389/fmicb.2015.00822;
RA   Mansor M., Hamilton T.L., Fantle M.S., Macalady J.L.;
RT   "Metabolic diversity and ecological niches of Achromatium populations
RT   revealed with single-cell genomic sequencing.";
RL   Front. Microbiol. 6:822-822(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00035577};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the GTP-binding SRP family.
CC       {ECO:0000256|ARBA:ARBA00008531}.
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:KOR29785.1}.
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DR   EMBL; JXSN01000147; KOR29785.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M1JAN1; -.
DR   PATRIC; fig|1604835.3.peg.529; -.
DR   Proteomes; UP000037003; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR   CDD; cd17874; FtsY; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.120.140; Signal recognition particle SRP54, nucleotide-binding domain; 1.
DR   HAMAP; MF_00920; FtsY; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR   InterPro; IPR004390; SR_rcpt_FtsY.
DR   InterPro; IPR036225; SRP/SRP_N.
DR   InterPro; IPR000897; SRP54_GTPase_dom.
DR   InterPro; IPR042101; SRP54_N_sf.
DR   NCBIfam; TIGR00064; ftsY; 1.
DR   PANTHER; PTHR43134:SF7; CELL DIVISION PROTEIN FTSY HOMOLOG, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43134; SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA; 1.
DR   Pfam; PF00448; SRP54; 1.
DR   Pfam; PF02881; SRP54_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00962; SRP54; 1.
DR   SUPFAM; SSF47364; Domain of the SRP/SRP receptor G-proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00300; SRP54; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000313|EMBL:KOR29785.1};
KW   Cell division {ECO:0000313|EMBL:KOR29785.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037003}.
FT   DOMAIN          251..264
FT                   /note="SRP54-type proteins GTP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00300"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KOR29785.1"
SQ   SEQUENCE   279 AA;  29931 MW;  D6E2232D461B2B87 CRC64;
     HGRKTIDADL REELETLLIT ADVGVETTSR IINELTAKVK REALTDPAVL ATELRTSLLQ
     IITTCQTQVR SALPGKTQVI LMVGVNGAGK TTTIGKLAQR LQQEGNKVML AAGDTFRAAA
     VEQLQVWGQR NNVPVIAQQQ GSDSASVIFD ALQAANARGI DVLIADTAGR LHTKYNLMEE
     LAKIARVMKK IDPDAPHEVL LVIDATTGQN GLNQAIQFNS AIPLTGIVVT KLDGTAKGGI
     LFAIAHQLRI PIRFIGVGEA LEDLQPFDAN NFVDALFGK
//
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