ID A8SZN4_9VIBR Unreviewed; 635 AA.
AC A8SZN4;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=protein-N(pi)-phosphohistidine--D-fructose phosphotransferase {ECO:0000256|ARBA:ARBA00012799};
DE EC=2.7.1.202 {ECO:0000256|ARBA:ARBA00012799};
GN ORFNames=AND4_06119 {ECO:0000313|EMBL:EDP60470.1};
OS Vibrio sp. AND4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=314289 {ECO:0000313|EMBL:EDP60470.1, ECO:0000313|Proteomes:UP000005159};
RN [1] {ECO:0000313|EMBL:EDP60470.1, ECO:0000313|Proteomes:UP000005159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AND4 {ECO:0000313|EMBL:EDP60470.1,
RC ECO:0000313|Proteomes:UP000005159};
RX PubMed=20436956; DOI=10.1371/journal.pbio.1000358;
RA Gomez-Consarnau L., Akram N., Lindell K., Pedersen A., Neutze R.,
RA Milton D.L., Gonzalez J.M., Pinhassi J.;
RT "Proteorhodopsin phototrophy promotes survival of marine bacteria during
RT starvation.";
RL PLoS Biol. 8:E1000358-E1000358(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC fructose 1-phosphate(in) + L-histidyl-[protein];
CC Xref=Rhea:RHEA:49252, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:37721, ChEBI:CHEBI:58674,
CC ChEBI:CHEBI:64837; EC=2.7.1.202;
CC Evidence={ECO:0000256|ARBA:ARBA00001401};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:EDP60470.1}.
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DR EMBL; ABGR01000001; EDP60470.1; -; Genomic_DNA.
DR RefSeq; WP_009840928.1; NZ_ABGR01000001.1.
DR AlphaFoldDB; A8SZN4; -.
DR OrthoDB; 9782569at2; -.
DR Proteomes; UP000005159; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IEA:InterPro.
DR GO; GO:0022877; F:protein-N(PI)-phosphohistidine-fructose phosphotransferase system transporter activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR CDD; cd00211; PTS_IIA_fru; 1.
DR CDD; cd05569; PTS_IIB_fructose; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR InterPro; IPR036095; PTS_EIIB-like_sf.
DR InterPro; IPR013011; PTS_EIIB_2.
DR InterPro; IPR003501; PTS_EIIB_2/3.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013014; PTS_EIIC_2.
DR InterPro; IPR004715; PTS_IIA_fruc.
DR InterPro; IPR003353; PTS_IIB_fruc.
DR InterPro; IPR006327; PTS_IIC_fruc.
DR NCBIfam; TIGR00829; FRU; 1.
DR NCBIfam; TIGR00848; fruA; 1.
DR NCBIfam; TIGR01427; PTS_IIC_fructo; 1.
DR PANTHER; PTHR30505; FRUCTOSE-LIKE PERMEASE; 1.
DR PANTHER; PTHR30505:SF0; FRUCTOSE-LIKE PTS SYSTEM EIIBC COMPONENT-RELATED; 1.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR SUPFAM; SSF52794; PTS system IIB component-like; 1.
DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 293..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 416..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 449..472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 484..517
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 562..582
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 602..622
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..149
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000259|PROSITE:PS51094"
FT DOMAIN 164..259
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000259|PROSITE:PS51099"
FT DOMAIN 286..632
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000259|PROSITE:PS51104"
SQ SEQUENCE 635 AA; 65716 MW; 1AB4B7CF49A9A6CD CRC64;
MITKLINEDL IKLDLQATSK EDVFKELVAV LHAQGRISNQ VQFLADIKAR EELDNTGFEN
GVAIPHAKSA AVIEPAVVIG VSKSGIEYGA EDGLPSKLFF MIASPDGGDN HHIEVLAELS
SKLIEDGFID AFLSAANGQD ALALLLAKEE LQSMTDAPAN KGFIIGVTGC PAGVAHTYLA
AEALEKGAAA MGYEIKVETN GSIGVKNSPT AEEIERADAI IVACDKQVDM NRFSGKRVVK
TNVKAPIRDA QNLINEALSA PAYQVRTSSN AQASVASKAS QARSDLYRYL MNGVSHMIPF
VVTGGLLIAL ALAVGGQPSE AGMAIPEGSM WNQILNVGVV AFTLMIPILA GYIAYAIADR
PALAPGLIGG WIANNGSFYG AEAGTGFIGA IIAGLLVGYF VKWITSINFH KFIQPLVPIM
IAPITGSLFI AGLFIFVIGA PIASLMDGLT ALLTSLSTGN VVLLGIVLGG MAGFDMGGPF
NKVAFLFSVG MIASGQTQFM GAMACAIPVA PLGMALATAL GRKFDLFEES ETEAGKAAGA
MGLVGISEGA IPFAAQDPMS VIPANVFGSM VAAVMAFSFG ITNSVAHGGP VVALLGAMNH
PILAVICMAT GAVVTAVTCV TLKKVRKAKM VQAAA
//
