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Database: UniProt
Entry: A0A1V4B336_9PAST
LinkDB: A0A1V4B336_9PAST
Original site: A0A1V4B336_9PAST 
ID   A0A1V4B336_9PAST        Unreviewed;       288 AA.
AC   A0A1V4B336;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=UPF0761 membrane protein NCTC1659_00301 {ECO:0000256|HAMAP-Rule:MF_00672};
GN   Name=rbn {ECO:0000313|EMBL:STO59076.1};
GN   ORFNames=NCTC1659_00301 {ECO:0000313|EMBL:STO59076.1};
OS   Canicola haemoglobinophilus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Canicola.
OX   NCBI_TaxID=733 {ECO:0000313|EMBL:STO59076.1, ECO:0000313|Proteomes:UP000254329};
RN   [1] {ECO:0000313|EMBL:STO59076.1, ECO:0000313|Proteomes:UP000254329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC1659 {ECO:0000313|EMBL:STO59076.1,
RC   ECO:0000313|Proteomes:UP000254329};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00672};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00672}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the UPF0761 family. {ECO:0000256|HAMAP-
CC       Rule:MF_00672}.
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DR   EMBL; UGHF01000001; STO59076.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4B336; -.
DR   OrthoDB; 9808671at2; -.
DR   Proteomes; UP000254329; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   HAMAP; MF_00672; UPF0761; 1.
DR   InterPro; IPR023679; UPF0761_bac.
DR   InterPro; IPR017039; Virul_fac_BrkB.
DR   NCBIfam; TIGR00765; yihY_not_rbn; 1.
DR   PANTHER; PTHR30213; UNCHARACTERIZED; 1.
DR   PANTHER; PTHR30213:SF2; UPF0761 MEMBRANE PROTEIN YIHY; 1.
DR   Pfam; PF03631; Virul_fac_BrkB; 1.
DR   PIRSF; PIRSF035875; RNase_BN; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00672}; Hydrolase {ECO:0000313|EMBL:STO59076.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00672};
KW   Reference proteome {ECO:0000313|Proteomes:UP000254329};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00672};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00672}.
FT   TRANSMEM        30..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00672"
FT   TRANSMEM        93..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00672"
FT   TRANSMEM        133..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00672"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00672"
FT   TRANSMEM        203..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00672"
FT   TRANSMEM        236..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00672"
SQ   SEQUENCE   288 AA;  32255 MW;  C72186EC5D703078 CRC64;
     MSILLRNLVA FFKVFLYRFK QNKLNQAAGY LTYSTMLAFV PSIMVFFSIF AAFPVFNEVT
     GELKQFIFTN FAPSASDVVG EYIDQFVNNS KQMSAVGIIS LIVVALMLIN SIDRTLNSIW
     HDTSVRPAVF SFAIYWLILT LGPIIIATSI GISTYVTTFA TRTFEQDLGL PIGIKLLGLL
     PFFLTWFIFT ILYMVVPNKK VSVVHSAAGA LIAAVFFTLG KQAFTWYITN FPSYQLIYGA
     MATLPIMLLW IQLSWTAILL GAQLSAVLAD MRSLHCGDIQ IEQIKEKK
//
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