ID A0A1Z4VUD2_9GAMM Unreviewed; 519 AA.
AC A0A1Z4VUD2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Peptidase M23 {ECO:0000313|EMBL:BAZ95113.1};
GN ORFNames=FOKN1_2753 {ECO:0000313|EMBL:BAZ95113.1};
OS Thiohalobacter thiocyanaticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalobacterales;
OC Thiohalobacteraceae; Thiohalobacter.
OX NCBI_TaxID=585455 {ECO:0000313|EMBL:BAZ95113.1, ECO:0000313|Proteomes:UP000218765};
RN [1] {ECO:0000313|EMBL:BAZ95113.1, ECO:0000313|Proteomes:UP000218765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOKN1 {ECO:0000313|EMBL:BAZ95113.1,
RC ECO:0000313|Proteomes:UP000218765};
RA Oshiki M., Fukushima T., Kawano S., Nakagawa J.;
RT "Thiocyanate degradation by Thiohalobacter thiocyanaticus FOKN1.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP018052; BAZ95113.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4VUD2; -.
DR KEGG; ttc:FOKN1_2753; -.
DR OrthoDB; 9805070at2; -.
DR Proteomes; UP000218765; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR CDD; cd12797; M23_peptidase; 1.
DR Gene3D; 3.10.450.350; -; 2.
DR Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR InterPro; IPR045834; Csd3_N2.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR007340; Opacity-associatedA.
DR InterPro; IPR016047; Peptidase_M23.
DR PANTHER; PTHR21666:SF272; BLL1407 PROTEIN; 1.
DR PANTHER; PTHR21666; PEPTIDASE-RELATED; 1.
DR Pfam; PF19425; Csd3_N2; 1.
DR Pfam; PF04225; OapA; 1.
DR Pfam; PF01551; Peptidase_M23; 1.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000218765};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 150..231
FT /note="Opacity-associated protein A"
FT /evidence="ECO:0000259|Pfam:PF04225"
FT DOMAIN 244..363
FT /note="Csd3-like second N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19425"
FT DOMAIN 376..472
FT /note="Peptidase M23"
FT /evidence="ECO:0000259|Pfam:PF01551"
FT REGION 86..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 56523 MW; 73299009A90B9F63 CRC64;
MTYSSVIKKD YKSVLEPERG ARRRLHPLHW LVLGAVAVSG IFLYTSAPEQ ASANLESAQP
ETAGTAAEQA LDSIYKQDII ALPGQAAPAP ASASASASGE PEDAPGSARA APDQPESGTA
PRAIPVTAAP AESAPEARSA GIQAPTELPW REVTVNPGDS LARIFSRLDL SPRSLHEIIH
LSDETRRLTR IHPGEKLQVR IDDAQGIAAL RYEYDRMHAL LVSRTEDGGF EAREVIREPQ
RSQVTATAEI DSSLFLAGQD AGLTDNLIME LAGIFGWDID FALDIRKGDR FSVLYEELYL
EGEKIGTGEI LAAEFVSQGR TFRAVRYTTA EGRSDYYAPD GRSMRKAFLR TPVAFSRISS
RFNLKRKHPV LNRIRAHKGV DYAAPYGTPI KATGSGKIVF QGTKGGYGRT VILQHGTRYS
TLYAHMSRHA RGLKTGSRVQ QGQVIGYIGK SGLATGPHLH YEFRIDGAHR NPLTVDLPAA
EPIEARYRED FESTAAQLLA ELELAVPGTA SQVAMNRQE
//
