ID K9RFM5_9CYAN Unreviewed; 590 AA.
AC K9RFM5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:AFY56288.1};
GN ORFNames=Riv7116_3845 {ECO:0000313|EMBL:AFY56288.1};
OS Rivularia sp. PCC 7116.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Rivulariaceae;
OC Rivularia.
OX NCBI_TaxID=373994 {ECO:0000313|EMBL:AFY56288.1, ECO:0000313|Proteomes:UP000010380};
RN [1] {ECO:0000313|EMBL:AFY56288.1, ECO:0000313|Proteomes:UP000010380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7116 {ECO:0000313|EMBL:AFY56288.1,
RC ECO:0000313|Proteomes:UP000010380};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Rivularia sp. PCC 7116.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000256|ARBA:ARBA00010860}.
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DR EMBL; CP003549; AFY56288.1; -; Genomic_DNA.
DR RefSeq; WP_015119854.1; NC_019678.1.
DR AlphaFoldDB; K9RFM5; -.
DR STRING; 373994.Riv7116_3845; -.
DR KEGG; riv:Riv7116_3845; -.
DR PATRIC; fig|373994.3.peg.4103; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_031959_0_0_3; -.
DR OrthoDB; 9772024at2; -.
DR Proteomes; UP000010380; Chromosome.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR003646; SH3-like_bac-type.
DR PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00287; SH3b; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000010380};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..590
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003934849"
FT DOMAIN 224..283
FT /note="SH3b"
FT /evidence="ECO:0000259|SMART:SM00287"
FT DOMAIN 471..583
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 590 AA; 64849 MW; 6983231B699A6CC4 CRC64;
MKPLLGFVVL ASIATPNLAW AQEQPLKVVY PPTNHKTTSD KIFFIGTAPP TGQVLINGKS
ITRSQSGHFA PSFPLQIGEN TFTIRHSDQQ VEIKVIRTST QPEVPQGLNF AKDSLTPKVD
IARLPGELIC FSAIAPPSAT VSVNFGDNKR VPLVLQPPQA QLPSNLAALT GTNQPQNATK
SEYSGCTMAE ANQLATPKYQ LTLNSQTITQ EAPGKITVLQ PSNLPVVEVS AEFGVARTGP
STNYSRLTPL PKGTRSAVTG KTGEWLRLDY GAWIKSSETV ALPNAIVPNT IIRSVASSQS
QDSTLVNFPL QTPVPVSVKQ ESDKLTLTLH NTTAQTDTIP FNDNPFISRM DWQQIPPSPG
VNSGAVQYIF NLKKNQQWGY KLGYEGTTLK LKLRHAPELR RSRRKPLSGI KILIDPGHGG
KELGAVGPTG LPEKDVNLTV SKLLRQELEK KGATVVMTRE VDKFVSLGDR QKIIAREEPT
LALSVHYNAL PDYGDAENTK GIGMFWYHPQ AHSLAIYLHN YLVKKLDRPS YGVFWNNLAL
TRPEAAPSLL LELGFMSNPE EFEWVNNPKQ QKKLARTLAD GIVKWLRDNR
//
