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Database: UniProt
Entry: F9HN61_STRMT
LinkDB: F9HN61_STRMT
Original site: F9HN61_STRMT 
ID   F9HN61_STRMT            Unreviewed;       750 AA.
AC   F9HN61;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Penicillin-binding protein 2X {ECO:0000313|EMBL:EGP68331.1};
GN   Name=pbpX {ECO:0000313|EMBL:EGP68331.1};
GN   ORFNames=HMPREF9957_1310 {ECO:0000313|EMBL:EGP68331.1};
OS   Streptococcus mitis SK1080.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1008453 {ECO:0000313|EMBL:EGP68331.1, ECO:0000313|Proteomes:UP000004568};
RN   [1] {ECO:0000313|EMBL:EGP68331.1, ECO:0000313|Proteomes:UP000004568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK1080 {ECO:0000313|EMBL:EGP68331.1,
RC   ECO:0000313|Proteomes:UP000004568};
RA   Durkin A.S., Radune D., Hostetler J., Torralba M., Gillis M., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC       Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family.
CC       {ECO:0000256|ARBA:ARBA00007171}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGP68331.1}.
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DR   EMBL; AFQV01000021; EGP68331.1; -; Genomic_DNA.
DR   RefSeq; WP_000872307.1; NZ_AFQV01000021.1.
DR   AlphaFoldDB; F9HN61; -.
DR   PATRIC; fig|1008453.3.peg.1131; -.
DR   eggNOG; COG0768; Bacteria.
DR   OrthoDB; 9804124at2; -.
DR   Proteomes; UP000004568; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   CDD; cd06573; PASTA; 2.
DR   Gene3D; 2.20.70.70; -; 2.
DR   Gene3D; 3.30.70.2110; -; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR005543; PASTA_dom.
DR   InterPro; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   NCBIfam; NF038271; strep_PBP2X; 1.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 1.
DR   Pfam; PF03793; PASTA; 1.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SMART; SM00740; PASTA; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR   SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 2.
DR   PROSITE; PS51178; PASTA; 2.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          632..691
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          692..750
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
SQ   SEQUENCE   750 AA;  82501 MW;  C093E5B6CC70899A CRC64;
     MKWTKRVIRY ATKNRKSPAE NRRRVGKSLS LLSVFVFAVF LVNFAVIIGT GTRFGTDLAK
     EAKKVHQTTR TVPAKRGTIY DRNGVPIAED ATSYNVYAVI DENYKSATGK ILYVEKTQFN
     KVAEVFHKYL DMEESYVREQ LSQPNLKQVS FGSKGNGITY ANMMAIKKEL ETAEVKGIDF
     TTSPNRSYPN GQFASSFIGL AQLHENEDGS KSLLGTSGME SSLNRILAGT DGIITYEKDR
     LGNIVPGTEQ VSQQTVDGKD VYTTISSTLQ SFMETQMNAF QEKVKGKYMT ATLVSAKTGE
     ILATTQRPTF DADTKEGLTK DFVWRDILYQ SNYEPGSTMK VMTLASSIDN NTFPSGEYFN
     SSELKIADVT IRDWDVNDGL TTGRMMTFLQ GFALSSNVGM SLLEQKMGDT TWLDYLNRFK
     FGVPTRFGLT DEYAGQLPAD NIVNIAQSSF GQGISVTQTQ MIRAFTAIAN DGVMLEPKFI
     SAIYDPNDQT ARKSQKEVVG NPVSKDAASL TRTNMILVGT DPVYGTMYNH STGKPTVTVP
     GQNVALKSGT AQIADEKNGG YLVGLTNYIF SAVSMNPAEN PDFILYVTVQ QPEHYSGIQL
     GEFANPILER ASAMKDSLNL QTTAKALEQV SQQSPYPMPS VKDISPGDLA EELRRNLVQP
     IVVGTGTKIK NSSAEEGKNL APNQQVLILS DKAEEVPDMY GWTRATAETF AKWLNIDLEF
     EGSGSTVQKQ DVRANTAIKG IKKITLTLGD
//
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