ID A0A0P6WGY5_9SPHN Unreviewed; 613 AA.
AC A0A0P6WGY5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=PEP-utilizing protein mobile subunit {ECO:0000313|EMBL:KPL68607.1};
GN ORFNames=SZ64_11130 {ECO:0000313|EMBL:KPL68607.1};
OS Erythrobacter sp. SG61-1L.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1603897 {ECO:0000313|EMBL:KPL68607.1, ECO:0000313|Proteomes:UP000049978};
RN [1] {ECO:0000313|EMBL:KPL68607.1, ECO:0000313|Proteomes:UP000049978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG61-1L {ECO:0000313|EMBL:KPL68607.1,
RC ECO:0000313|Proteomes:UP000049978};
RA Palumuru S., Dellas N., Pearce S.L., Warden A.C., Oakeshott J.G.,
RA Pandey G.;
RT "Phylogenetic and kinetic characterization of a suite of dehydrogenases
RT from a newly isolated bacterium, strain SG51-1L, that catalyze the turnover
RT of guaiacylglycerol-beta-guaiacyl ether stereoisomers.";
RL Appl. Environ. Microbiol. 0:0-0(2015).
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:KPL68607.1}.
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DR EMBL; JXQC01000003; KPL68607.1; -; Genomic_DNA.
DR RefSeq; WP_054532206.1; NZ_JXQC01000003.1.
DR AlphaFoldDB; A0A0P6WGY5; -.
DR STRING; 1603897.SZ64_11130; -.
DR PATRIC; fig|1603897.4.peg.2157; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000049978; Unassembled WGS sequence.
DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR PANTHER; PTHR43615; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43615:SF1; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000049978}.
FT DOMAIN 528..599
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 613 AA; 69405 MW; 5356D2CBA0880C04 CRC64;
MADEAKGFPL PSSLKVVPGT EAAQAAYPYY TQFTPEDDER FWFYNSMHFP EPMHHFDMIT
AEAAYVALGA FNTRVHVLPT AKGIDHRVIN GRVYIGGVAV TDPAEIEERV GEFQQRAFYY
YEHWETLYDQ WKDKMKALIA DAQALPKPSL PDYEPLETTH TGKGVAANHA LLDIYQKQIE
GYHRMWHHHF EFLLLGYGAY MTFFDFCKKA FPEISDQTIS RMVAGMEAEI FRPDEEVKRL
ARRAVELGVD DKFHDGMYID DVLEALDQLG ESGKAWLDEL EASRNPWFNV SSGDGFYHYH
RSWNDDLSLP FAALPGYIEK VKAGTNIERP TGQLVAEREQ LVADYRDLLD TNEDKATYDQ
LIHLAHRVFP YVEGHKFYCE HWYTNLFFNK IREFGALLRD HGFFEKEEDV FHLTQYELES
AIIDLMLSWG IGSEPRGPKY WPAIVKQRAA AIAEWAKHPT PPALGNVPDS IDDPAIVMLW
GITRDNLDTW LNADADEDTR ELKGFAACHG VVEGPARVVK SVEEIGRLQQ GDILVCQVTN
PTWAPIFQKI SAAVSDIGGS MSHMAIVARE YGLPAVVGTG TATQKIKDGQ RIRVDGGRGT
VTILDEETVL EDA
//
