ID U1JR99_9GAMM Unreviewed; 442 AA.
AC U1JR99;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Cell division transporter substrate-binding protein {ECO:0000313|EMBL:ERG19527.1};
DE Flags: Fragment;
GN ORFNames=PCIT_06650 {ECO:0000313|EMBL:ERG19527.1};
OS Pseudoalteromonas citrea DSM 8771.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1117314 {ECO:0000313|EMBL:ERG19527.1, ECO:0000313|Proteomes:UP000016487};
RN [1] {ECO:0000313|EMBL:ERG19527.1, ECO:0000313|Proteomes:UP000016487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8771 {ECO:0000313|Proteomes:UP000016487};
RX PubMed=22535931; DOI=10.1128/JB.00265-12;
RA Xie B.B., Shu Y.L., Qin Q.L., Rong J.C., Zhang X.Y., Chen X.L., Shi M.,
RA He H.L., Zhou B.C., Zhang Y.Z.;
RT "Genome sequences of type strains of seven species of the marine bacterium
RT Pseudoalteromonas.";
RL J. Bacteriol. 194:2746-2747(2012).
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:ERG19527.1}.
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DR EMBL; AHBZ02000070; ERG19527.1; -; Genomic_DNA.
DR AlphaFoldDB; U1JR99; -.
DR STRING; 1117314.PCIT_06650; -.
DR eggNOG; COG0552; Bacteria.
DR OrthoDB; 9804720at2; -.
DR Proteomes; UP000016487; 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 SMART; SM00963; SRP54_N; 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:ERG19527.1};
KW Cell division {ECO:0000313|EMBL:ERG19527.1};
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:UP000016487}.
FT DOMAIN 412..425
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT REGION 1..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ERG19527.1"
SQ SEQUENCE 442 AA; 48735 MW; D45851ADE02F3573 CRC64;
TEQEAERQRL EAEAQAKLEQ ESIEAEKQAA EQEAERQRLE AEAQAKLEQE RIEAEKQAAE
QEAERQRLEA EAQAKLEQER LAAEKQAAEQ EAERQRLEAE AKLEQERLAA EKQAAEQEAK
AKLDAEQAAN KEKPKKEGFF ARLKKGLLKT KVNLGSGIAS IFKGKKIDDD LFEELETQLL
TADLGVDTTM KLIDSLTDAA DRKQLKDGDA LYELMKQEMA EMLKEAEKPL EIPENKKPFV
ILMVGVNGVG KTTTIGKLAK QFQQEGKSVM LAAGDTFRAA AVEQLQVWGE RNDISVIAQH
TGADSASVVF DAFQAAQARN VDVLIADTAG RLQNKDNLMQ ELEKIARVMK KLDPDAPHEV
MLTIDAGTGQ NAISQVNLFN QAVGLTGIAL TKLDGTAKGG VIFAVADKFQ VPIRYIGVGE
GIDDLRTFKS DDFIDALFSQ DD
//
