ID G2IIB7_SPHSK Unreviewed; 632 AA. AC G2IIB7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 24-JAN-2024, entry version 46. DE SubName: Full=Putative M2 family peptidase {ECO:0000313|EMBL:BAK67040.1}; GN ORFNames=SLG_23650 {ECO:0000313|EMBL:BAK67040.1}; OS Sphingobium sp. (strain NBRC 103272 / SYK-6). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=627192 {ECO:0000313|EMBL:BAK67040.1, ECO:0000313|Proteomes:UP000001275}; RN [1] {ECO:0000313|EMBL:BAK67040.1, ECO:0000313|Proteomes:UP000001275} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 103272 / SYK-6 {ECO:0000313|Proteomes:UP000001275}; RX PubMed=22207743; DOI=10.1128/JB.06254-11; RA Masai E., Kamimura N., Kasai D., Oguchi A., Ankai A., Fukui S., RA Takahashi M., Yashiro I., Sasaki H., Harada T., Nakamura S., Katano Y., RA Narita-Yamada S., Nakazawa H., Hara H., Katayama Y., Fukuda M., RA Yamazaki S., Fujita N.; RT "Complete genome sequence of Sphingobium sp. strain SYK-6, a degrader of RT lignin-derived biaryls and monoaryls."; RL J. Bacteriol. 194:534-535(2012). 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; AP012222; BAK67040.1; -; Genomic_DNA. DR RefSeq; WP_014076685.1; NC_015976.1. DR AlphaFoldDB; G2IIB7; -. DR STRING; 627192.SLG_23650; -. DR KEGG; ssy:SLG_23650; -. DR eggNOG; COG1164; Bacteria. DR HOGENOM; CLU_014364_3_0_5; -. DR OrthoDB; 5241329at2; -. DR Proteomes; UP000001275; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro. DR GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR CDD; cd06461; M2_ACE; 1. DR Gene3D; 1.10.1370.30; -; 2. DR InterPro; IPR001548; Peptidase_M2. DR PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1. DR PANTHER; PTHR10514:SF27; ANGIOTENSIN-CONVERTING ENZYME; 1. DR Pfam; PF01401; Peptidase_M2; 1. DR PRINTS; PR00791; PEPDIPTASEA. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. PE 4: Predicted; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Reference proteome {ECO:0000313|Proteomes:UP000001275}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 25..632 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5003431312" SQ SEQUENCE 632 AA; 70202 MW; 99041DA3CB782654 CRC64; MHILVSRIAL SAAMLLAAPA AVLAQAGQGQ KAPDSAQADA FVAAAEKEAF DYSVDASRIM WVNATHITDD TDALAAQAGA KGTEMAVRFA LEAAKYEQVP GLSFDTKRKL DIMRSGIVLP APTKPGAAAE LNEIATRLQS TYGKGRGTLD GKELTGSDIE AEMANLSHTP AQFSEMWTSW HDRVGAPMKA DYVRLVDIAN EGAKELGFAD AGAMWRSGYD MPPDEFAALT EALWQEVKPL YDALHCYTRT KLNEKYGDAV QSPTGPIRAD LLGNMWAQEW GNIYPIVAPA GTGDLGYDIG DLLRAKGFVQ TTPQTIDTPD TPETQRRGYW EKQMFRIGEG FYSSLGFDPL PETFWQRTQF IAPRDREVVC HASAWDVDNR NDIRVKMCTK VNSDDFVTIH HELGHNYYQR AYQKHGYLYL NGANDGFHEA IGDFIALSIT PQYLVQIGLL DPAKVPSADK DIGLLLRQAM DKVAFLPFGL LIDRWRWGVF DGSIRPADYN KAWTDMRLRY QGIVPPTDRP ADSFDPGAKF HVPGNTPYTR YFLARILQFQ FYEAACRQAG WKGPLHRCSF YGNKEVGKRL NAMLEMGASK PWPDALEAFT GSRKMSGKAM LAYFAPLGKW LDQQNKGKQC GW //