ID B8E3Q8_SHEB2 Unreviewed; 1062 AA.
AC B8E3Q8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ACK44559.1};
DE Flags: Precursor;
GN OrderedLocusNames=Sbal223_0015 {ECO:0000313|EMBL:ACK44559.1};
OS Shewanella baltica (strain OS223).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=407976 {ECO:0000313|EMBL:ACK44559.1, ECO:0000313|Proteomes:UP000002507};
RN [1] {ECO:0000313|Proteomes:UP000002507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS223 {ECO:0000313|Proteomes:UP000002507};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J., Konstantinidis K.,
RA Tiedje J.;
RT "Complete sequence of chromosome of Shewanella baltica OS223.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001252; ACK44559.1; -; Genomic_DNA.
DR RefSeq; WP_012586338.1; NC_011663.1.
DR AlphaFoldDB; B8E3Q8; -.
DR KEGG; sbp:Sbal223_0015; -.
DR HOGENOM; CLU_003547_0_0_6; -.
DR Proteomes; UP000002507; Chromosome.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR011659; PD40.
DR PANTHER; PTHR42972; TOL-PAL SYSTEM PROTEIN TOLB; 1.
DR PANTHER; PTHR42972:SF8; TOL-PAL SYSTEM PROTEIN TOLB; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF07676; PD40; 4.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ACK44559.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1062
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002870610"
FT DOMAIN 706..1038
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 1062 AA; 117479 MW; 7A16EDE3014F2B35 CRC64;
MLKSKLTPLY IALALGMNTL AVNAAETKKA EWNVNAPANA PLEQVKIDVS EGTWMNLSVS
PDGKNIVFDL LGDIYQIPVT GGEAKPLAQG IAWQMQPVYS PDGKHIAFTS DGDGGDNIWI
MDADGSNPRT VTQETFRLLN SPAWSPDSQY LVARKHFTAS RSLGAGEVWL YHVAGGEGVK
LTERPNDQKD LGEPAYSPDG RYIYFSQDDT PGKTFHYSKD SVNGIYKIKR YDTQTGDIEI
LIEGTGGAIR PTPSPDGTKL AYIKRDDFNS SLYLLDLKSG ETTKLFGELD RDMQETWAIH
GVYPTMAWTL DNKDIFFWAK GKINRLNVAS KTLTDIPFSV KTELAVQPSV RFKQDIDKDV
FDVKMLRMAQ VSPDGSKVAF EALGKIWLKS LPDGKMSRLT ELNNGIEELY PQWSRDGKNI
VFTTWNDQDQ GTVQVISAKG GKPKQLTSEP GKYEEPTFSP DGELVVYRKT QGGNLTPRTW
SQEPGLYKVD IKGKQNKKIS ADGYQAQFGA NADRVFFMNS SEDETPQLSS INLDGFDKRV
HYSSKHATEF RVSPDGGQLA FAERFKVWVT PFAKHGETVE IGPNANNLPV SQLSIRAGES
ISWNSKSNQL YWTLGPELYQ AKVDTQYLNK DEKAQPSIIN LGFTEKADVP RGTIAFVGGK
VITMENDQVI DNGVVIVKDN HIVAVGNANI AIPKDAQIID IKGKSIMPGL FDAHAHGPQA
DDEIVPQQNW ALYSGLSLGV TTIHDPSNDT TEIFAASEQQ KAGHIVGPRI FSTGTILYGA
NAPGYTSHID SLDDAKFHLE RLKKVGAFSV KSYNQPRRNQ RQQVIAAARE LEMMVVPEGG
SLLQHNLTMV ADGHTTVEHS LPVAAIYNDI KQFWSQTKVG YTPTLVVAYG GISGENYWYD
KTDVWAHPRL SMYVPADILQ ARSMRRPHAP DGHYNHFNVA KVANELNKLG VHPNIGAHGQ
REGLAAHWEM WMFAQGGMSN MEVLKTATIN PATTFGMEQQ LGSIKAGKLA DLIVIDGDPL
ADIRVTDKVT YTMVNGKLFD AETMNELNGD KEKRKPFFFE KI
//