ID A0A0S2JZF2_9GAMM Unreviewed; 1057 AA.
AC A0A0S2JZF2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ALO41575.1};
GN ORFNames=PP2015_1058 {ECO:0000313|EMBL:ALO41575.1};
OS Pseudoalteromonas phenolica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=161398 {ECO:0000313|EMBL:ALO41575.1, ECO:0000313|Proteomes:UP000061457};
RN [1] {ECO:0000313|EMBL:ALO41575.1, ECO:0000313|Proteomes:UP000061457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 12086 {ECO:0000313|EMBL:ALO41575.1,
RC ECO:0000313|Proteomes:UP000061457};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TolB family.
CC {ECO:0000256|ARBA:ARBA00009820}.
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DR EMBL; CP013187; ALO41575.1; -; Genomic_DNA.
DR RefSeq; WP_058029302.1; NZ_CP013187.1.
DR AlphaFoldDB; A0A0S2JZF2; -.
DR STRING; 161398.PP2015_1058; -.
DR KEGG; pphe:PP2015_1058; -.
DR PATRIC; fig|161398.10.peg.1078; -.
DR OrthoDB; 6188902at2; -.
DR Proteomes; UP000061457; Chromosome I.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 1.20.58.520; Amidohydrolase; 1.
DR Gene3D; 3.30.110.90; Amidohydrolase; 1.
DR Gene3D; 3.40.50.10910; Amidohydrolase; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 3.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
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; PTHR36842; PROTEIN TOLB HOMOLOG; 1.
DR PANTHER; PTHR36842:SF1; TOL-PAL SYSTEM PROTEIN TOLB; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF07676; PD40; 5.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR SUPFAM; SSF69304; Tricorn protease N-terminal domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:ALO41575.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000061457};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1057
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006600930"
FT DOMAIN 972..1036
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 1057 AA; 117366 MW; 0469575A175AF413 CRC64;
MKKQFYSALA LSVSLALGSA QAAEKSEKWQ VDAPQGEFFD AKVSVEQGTW MNVDVSPDGK
TIVFDLLGDI YTMPMKGGKA TQLTSDIGWQ MQPRFSPDGQ YIAFTSDQGG GDNIWVMKTD
GSEQTAVTKE TFRLLNSPSW SPDGNFIVAR KHFTGTRSLG AGEVWMYHKS GGNGVQLTKR
PNEQKDLGEP AFSPDGRYVY FSQDATPGKT FHYSKDSVAG IYKIKRLDRE TGEIEVILSG
MGGAIRPTPS PDGKTLAYIK RDDFQSSLYL YDLESGEHTK LYGELERDMQ ETWAIHGVYP
TIAWTPDQKH LVFWAGGKIH KLAVKNKSVE EIAFKVETTK KLQKALRFAQ DIDEPEFDVK
MLRNVQVSPD GETAIFEAMG HIYKRDLESG KIKRLTKQKD HFEFFPQFSR DGKKIVYVTW
DDKEQGSVRV VSARSGRGKA VTKQPGKYVE PTFSPDGDTV VYRKTSGSSI LTPEWSLKSG
IYTVSSKGGE SELITESGFQ PQFADRNDRI FVMAGWPKPQ FRAVNLETKK TQVLYESKHA
TEYRVSPDGK YLAFAERFKV FVTPFVESGK TINISPSDKQ FPVEQLSVRA GEGISWSAKG
DKLYWSLGPE LYHASLAGMF DINKAEDADF KVASGTNIGF KQKMAEPKGM IALTGATIVT
MKGEQVIENG VVLTDGKHIK AVGPQADVRI PKGAKVIDVT GKTILPGLVD VHAHGAQGSN
EIIPEQNWKN FAGLSLGVTT IHDPSNDTTE IFAASEMQKA GKIVGPRIFS TGTILYGANM
PGYTSHVDSL DDAKFHLERL QKVGAFSVKS YNQPRREQRQ QVVEAGRQLG MMVVPEGGSL
LQHNLTMVVD GHTGIEHSLP VSHIYDDIKQ LWSQTDVGYT PTLGVAYGGI WGENYWYDKT
DVWAHPRLSK FVPKNQLLPR SMRRIKSPDH HYNHFNNARV SAELQDLGAL VNLGAHGQRE
GLAAHWEIWM FAQGGMTPHE ALRAATIDPA KHIGLDEHIG SIEAGKLADL IVLDKNPLDN
IRDTDKISHT MINGRLFDAS TMQEVGAKKR EKLFFEE
//
