ID B3ES86_AMOA5 Unreviewed; 422 AA.
AC B3ES86;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Polysaccharide biosynthesis protein C-terminal domain-containing protein {ECO:0000259|Pfam:PF14667};
GN OrderedLocusNames=Aasi_0699 {ECO:0000313|EMBL:ACE06088.1};
OS Amoebophilus asiaticus (strain 5a2).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Amoebophilaceae;
OC Candidatus Amoebophilus.
OX NCBI_TaxID=452471 {ECO:0000313|EMBL:ACE06088.1, ECO:0000313|Proteomes:UP000001227};
RN [1] {ECO:0000313|EMBL:ACE06088.1, ECO:0000313|Proteomes:UP000001227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5a2 {ECO:0000313|EMBL:ACE06088.1,
RC ECO:0000313|Proteomes:UP000001227};
RX PubMed=20023027; DOI=10.1128/JB.01379-09;
RA Schmitz-Esser S., Tischler P., Arnold R., Montanaro J., Wagner M.,
RA Rattei T., Horn M.;
RT "The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus'
RT reveals common mechanisms for host cell interaction among amoeba-associated
RT bacteria.";
RL J. Bacteriol. 192:1045-1057(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP001102; ACE06088.1; -; Genomic_DNA.
DR RefSeq; WP_012472855.1; NC_010830.1.
DR AlphaFoldDB; B3ES86; -.
DR STRING; 452471.Aasi_0699; -.
DR KEGG; aas:Aasi_0699; -.
DR eggNOG; COG2244; Bacteria.
DR HOGENOM; CLU_022017_0_2_10; -.
DR OrthoDB; 9815702at2; -.
DR Proteomes; UP000001227; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR029303; Polysacc_synt_C.
DR InterPro; IPR002797; Polysacc_synth.
DR PANTHER; PTHR43424; LOCUS PUTATIVE PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR43424:SF1; LOCUS PUTATIVE PROTEIN 1-RELATED; 1.
DR Pfam; PF01943; Polysacc_synt; 1.
DR Pfam; PF14667; Polysacc_synt_C; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001227};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 365..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 389..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 339..415
FT /note="Polysaccharide biosynthesis protein C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14667"
SQ SEQUENCE 422 AA; 47900 MW; 6F7841360E481555 CRC64;
MHQDTKIFLA NFFQLSFLRG ISRILPLITT PFLIRVIGIE KFGTLEFAKA ISFYFTIFVS
YGFRFSATKQ VSLYKQDKNI IGQIVSSVYL LKLLIIVICF LIMIMLIVFV PKIREERIYL
LCFFPVVIAS SLFPTFAFQG LDKMHWLTSL NLISKVLFMA SLFIFIGKPS DAFLFPILLA
AVDILRLLVA FFVLYVSLTI PVRWPVWSIM KQQMKEGLHI FLSELAIMFY SRFPTIFLKF
VGGSTIVAIY TLGDKIARIT AGMLEPFMQA LYPIAYQKIT SNLEVGIQYL KYLAKSSLIV
LGVIGVVYWL FADKIIWLLA HTDLPEAVEV FKIHAFLPAI VFLSKLLGIG ILIPLQAGRK
YTLSILLTGL IAVGLHFILV PLFQVKGAAW SIVLSEVFAV IFTCLATYKE INILKINNQL
KH
//
