ID A0A0U4X2Z1_9GAMM Unreviewed; 952 AA.
AC A0A0U4X2Z1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:ALZ74361.1};
GN ORFNames=ATY27_00300 {ECO:0000313|EMBL:ALZ74361.1};
OS Rheinheimera sp. F8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=1763998 {ECO:0000313|EMBL:ALZ74361.1, ECO:0000313|Proteomes:UP000059499};
RN [1] {ECO:0000313|Proteomes:UP000059499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F8 {ECO:0000313|Proteomes:UP000059499};
RA Schuster A.K., Szewzyk U.;
RT "Draft genome sequence of Rheinheimera sp. F8, a biofilm-forming strain
RT which produces large amounts of extracellular DNA.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALZ74361.1, ECO:0000313|Proteomes:UP000059499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F8 {ECO:0000313|EMBL:ALZ74361.1,
RC ECO:0000313|Proteomes:UP000059499};
RX PubMed=26966195;
RA Schuster A.K., Szewzyk U.;
RT "Draft Genome Sequence of Rheinheimera sp. F8, a Biofilm-Forming Strain
RT Which Produces Large Amounts of Extracellular DNA.";
RL Genome Announc. 4:0-0(2016).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; CP013656; ALZ74361.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U4X2Z1; -.
DR Proteomes; UP000059499; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF35; NON-CATALYTIC MEMBER OF PEPTIDASE SUBFAMILY M16B-RELATED; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000059499};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..952
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006853777"
FT DOMAIN 64..199
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 222..398
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 535..671
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 690..864
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 952 AA; 105026 MW; 96248BEF7E25A2AB CRC64;
MKRFALSVLS LSLLLAGCQQ AALSPQPTAN QLPAGIELIK DASVSSSSVA IPYKKYRLAN
GLTVVVHEDQ SDPLVHVDVT YHVGSAREEP GKSGFAHFFE HMMFQGSEHV ADEQHFKIIT
EAGGEMNGST NSDRTNYYQT VPVNQLEKVL WLESDRMGFL LDAVTEKKFE VQRETVKNER
GQSVDNRPYG RLSERVAQAF YPDGHPYSWP VIGHMADLNR ANVNDVKAFF LRWYGPNNAT
LTIGGAVKAE DILPLVQQYF AAIPRGPEVT PTAKTAVSLT ADRYVSMEDN VHLPLLYMAF
PTVYARHEDE AALDILAEIL GGGNNSLLYK NLVKTQKAVQ AQTGHGCQEL ACEFTLLALP
APGAVKSLAE TEQQIRQSLA EFEQRGVTDD DLNKVKAKME AASIFALQSV EGKVSRLAAN
ETFFGEPDLA AADLTRYQRV TKADVTRVYQ QYLKGKAAVV MSVVPKGQRQ LIAKADNFTP
VTHDFGGPST TKAEDLQLRR AQDTLDRSKI PGAGANPAVT LPATWQQQLN NGIRVLGAQS
HETPTTSLLL RVPLGLYDET PQQAGISQLL AAMLDESTML KTTEQMSLAL EKLGASISFS
AGDEYLEVTV QSLSKHLPQT LELLMEKLLL PAFNTEDFSR AQQQTLQFIQ HSEKDAGFLA
SRAVQQLMFG NHISAYPNQG TLQSVSALKI TDIKTYAQRL LKPAHAELIL VSDLPQAQVL
AELQPRLQRW LGEAPTRQVQ IPNAVAKTGT IYLIDKPDAP QSEIRIVKRS LSRDFTGEYF
RSGLMNFVLG GNFNSRINLN LREDKGYTYG ANSYFSADRY AGIYQAAAAV RADVTGASVQ
EFFKELSRYQ QQGMTPQELD FMRKAINQAD ALAYETPGAK LGFMSAILQY GLASDFTTQR
NQIVRDITLD ELNQLAKRHL DPASFSVVIV GPAAQVRPQL EKLGMPVENY QF
//