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Database: UniProt
Entry: A3TZ68_PSEBH
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ID   A3TZ68_PSEBH            Unreviewed;       747 AA.
AC   A3TZ68;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE            EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN   ORFNames=OB2597_15930 {ECO:0000313|EMBL:EAQ02886.1};
OS   Pseudooceanicola batsensis (strain ATCC BAA-863 / DSM 15984 / KCTC 12145 /
OS   HTCC2597) (Oceanicola batsensis).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudooceanicola.
OX   NCBI_TaxID=252305 {ECO:0000313|EMBL:EAQ02886.1, ECO:0000313|Proteomes:UP000004318};
RN   [1] {ECO:0000313|EMBL:EAQ02886.1, ECO:0000313|Proteomes:UP000004318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-863 / DSM 15984 / KCTC 12145 / HTCC2597
RC   {ECO:0000313|Proteomes:UP000004318};
RX   PubMed=20418400; DOI=10.1128/JB.00412-10;
RA   Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.;
RT   "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola
RT   batsensis HTCC2597(TDelta).";
RL   J. Bacteriol. 192:3549-3550(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-
CC         L-histidyl-[protein] + pyruvate; Xref=Rhea:RHEA:23880, Rhea:RHEA-
CC         COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:15361, ChEBI:CHEBI:29979,
CC         ChEBI:CHEBI:58702, ChEBI:CHEBI:64837; EC=2.7.3.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00000683};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007837}.
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:EAQ02886.1}.
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DR   EMBL; AAMO01000006; EAQ02886.1; -; Genomic_DNA.
DR   RefSeq; WP_009807395.1; NZ_CH724131.1.
DR   AlphaFoldDB; A3TZ68; -.
DR   STRING; 252305.OB2597_15930; -.
DR   eggNOG; COG3605; Bacteria.
DR   HOGENOM; CLU_007308_7_2_5; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000004318; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR   Gene3D; 1.10.274.10; PtsI, HPr-binding domain; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR000121; PEP_util_C.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR006318; PTS_EI-like.
DR   InterPro; IPR008731; PTS_EIN.
DR   InterPro; IPR036618; PtsI_HPr-bd_sf.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   NCBIfam; TIGR01417; PTS_I_fam; 1.
DR   PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR   PANTHER; PTHR46244:SF3; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF05524; PEP-utilisers_N; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   PRINTS; PR01736; PHPHTRNFRASE.
DR   SMART; SM00065; GAF; 1.
DR   SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW   Pyruvate {ECO:0000313|EMBL:EAQ02886.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004318};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EAQ02886.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          25..171
FT                   /note="GAF"
FT                   /evidence="ECO:0000259|SMART:SM00065"
SQ   SEQUENCE   747 AA;  82689 MW;  EFBFE4ACB0303E60 CRC64;
     MSDDFQTDSQ QMLARLRVAM AEEAAGQERL DKITHLIADS MRTEVCSVYL FRDFDTLELC
     ATEGLKAEAV HQTRMRLGEG LVGRVGRTGR IINTPDAPSE PGFRYMPETG EEIYSSFAGV
     PIQRLGEKLG VLVVQSKVAR RYAEDEITAL EVVAMVLAEM AELGAFVGEG AALTALHTKP
     VVFRGATAQE GSAEGHVWLH EPRVVITNPI AEDPHRERER LAAAVDQLRD SVDAMVLGIA
     DDDKEQLEIL EAYRMFANSK GWLRRMEEDI ARGLSAEAAV EKEQSQARAR MESITDPYLR
     GRLHDLDDLS NRLLRILSGQ GKETGADMPA DPILVARNIG PAELLDYGRS LKGIVLEEGS
     VGSHAAIVAR ALAIPLIIHA DRITTEALNR DHILVDGDSG LAHLRPEETV ITAFRDKMAM
     QAKAQERYAS IRDLPAVTMC GERLHLAMNA GLMADLPSLA GSGAEGVGLF RTELQFLIRN
     QMPRRSELSA LYARVMDAAE GRKVVFRTLD IGSDKVLSYM KPTEEPNPAL GWRAIRVGLD
     KPGVMRMQLQ ALIRAANGRP LTVMFPFVAQ YEEYRAACAE MDKALDRERI LGHPIPEPLE
     VGAMLETPSL AFAPRRFFEE VQFLSIGGND LKQFFFAADR ENERVRRRYD TLNVSFLTFL
     QGIVDRCTET GTPLSFCGED AGRPVEAICL AAMGLRTLSM RPASIGPVKS LLMRTDLRAL
     REVIDRARDE GRQSVRDPVM EFLRNQG
//
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